Accepted name: 4-acetamidobutyryl-CoA deacetylase
Reaction: 4-acetamidobutanoyl-CoA + H2O = acetate + 4-aminobutanoyl-CoA
Other name(s): aminobutyryl-CoA thiolesterase; deacetylase-thiolesterase
Systematic name: 4-acetamidobutanoyl-CoA amidohydrolase
Comments: The enzyme also hydrolyses 4-aminobutanoyl-CoA to aminobutanoate and coenzyme A.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Ohsugi, M., Khan, J., Hensley, C., Chew, S. and Barker, H.A. Metabolism of L-β-lysine by a Pseudomonas. Purification and properties of a deacetylase-thiolesterase utilizing 4-acetamidobutyryl CoA and related compounds. J. Biol. Chem. 256 (1981) 7642-7651. [PMID: 6788773]
Accepted name: peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase
Reaction: Hydrolysis of an N4-(acetyl-β-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-β-D-glucosaminylamine and a peptide containing an aspartate residue
Other name(s): glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase
Systematic name: N-linked-glycopeptide-(N-acetyl-β-D-glucosaminyl)-L-asparagine amidohydrolase
Comments: Does not act on (GlcNAc)Asn, because it requires the presence of more than two amino-acid residues in the substrate [cf. EC 3.5.1.26 N4-(β-N-acetylglucosaminyl)-L-asparaginase]. The plant enzyme was previously erroneously listed as EC 3.2.2.18.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 83534-39-8
References:
1. Plummer, T.H., Jr. and Tarentino, A.L. Facile cleavage of complex oligosaccharides from glycopeptides by almond emulsin peptide: N-glycosidase. J. Biol. Chem. 256 (1981) 10243-10246. [PMID: 7287707]
2. Takahashi, N. Demonstration of a new amidase acting on glycopeptides. Biochem. Biophys. Res. Commun. 76 (1977) 1194-1201. [PMID: 901470]
3. Takahashi, N. and Nishibe, H. Some characteristics of a new glycopeptidase acting on aspartylglycosylamine linkages. J. Biochem. (Tokyo) 84 (1978) 1467-1473. [PMID: 738997]
4. Tarentino, A.L., Gomez, C.M. and Plummer, T.H., Jr. Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F. Biochemistry 24 (1985) 4665-4671. [PMID: 4063349]
Accepted name: N-carbamoylputrescine amidase
Reaction: N-carbamoylputrescine + H2O = putrescine + CO2 + NH3
Other name(s): carbamoylputrescine hydrolase; NCP
Systematic name: N-Carbamoylputrescine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 85030-69-9
References:
1. Yanagisawa, H. and Suzuki, Y. Preparation and properties of N-carbamylputrescine amidohydrolase from maize shoots. Phytochemistry 21 (1982) 2201-2203.
Accepted name: allophanate hydrolase
Reaction: urea-1-carboxylate + H2O = 2 CO2 + 2 NH3
Glossary: allophanate = urea-1-carboxylate
Other name(s): allophanate lyase; AtzF; TrzF
Systematic name: urea-1-carboxylate amidohydrolase
Comments: Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) and EC 3.5.1.84 (biuret amidohydrolase), this enzyme forms part of the cyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 6.3.4.6, urea carboxylase, thus bringing about the hydrolysis of urea to CO2 and NH3 in the presence of ATP and bicarbonate. The enzyme from Pseudomonas sp. strain ADP has a narrow substrate specificity, being unable to use the structurally analogous compounds urea, hydroxyurea or methylcarbamate as substrate [6].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 79121-96-3
References:
1. Maitz, G.S., Haas, E.M. and Castric, P.A. Purification and properties of the allophanate hydrolase from Chlamydomonas reinhardii. Biochim. Biophys. Acta 714 (1982) 486-491.
2. Roon, R.J. and Levenberg, B. Urea amidolyase. I. Properties of the enzyme from Candida utilis. J. Biol. Chem. 247 (1972) 4107-4113. [PMID: 4556303]
3. Sumrada, R.A. and Cooper, T.G. Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast. J. Biol. Chem. 257 (1982) 9119-9127. [PMID: 6124544]
4. Kanamori, T., Kanou, N., Kusakabe, S., Atomi, H. and Imanaka, T. Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP-dependent degradation pathway specific to urea. FEMS Microbiol. Lett. 245 (2005) 61-65. [PMID: 15796980]
5. Cheng, G., Shapir, N., Sadowsky, M.J. and Wackett, L.P. Allophanate hydrolase, not urease, functions in bacterial cyanuric acid metabolism. Appl. Environ. Microbiol. 71 (2005) 4437-4445. [PMID: 16085834]
6. Shapir, N., Sadowsky, M.J. and Wackett, L.P. Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP. J. Bacteriol. 187 (2005) 3731-3738. [PMID: 15901697]
7. Shapir, N., Cheng, G., Sadowsky, M.J. and Wackett, L.P. Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth. Appl. Environ. Microbiol. 72 (2006) 2491-2495. [PMID: 16597948]
Accepted name: long-chain-fatty-acyl-glutamate deacylase
Reaction: N-long-chain-fatty-acyl-L-glutamate + H2O = a long-chain carboxylate + L-glutamate
Other name(s): long-chain aminoacylase; long-chain-fatty-acyl-glutamate deacylase; long-chain acylglutamate amidase; N-acyl-D-glutamate deacylase
Systematic name: N-long-chain-fatty-acyl-L-glutamate amidohydrolase
Comments: Does not act on acyl derivates of other amino acids. Optimum chain length of acyl residue is 12 to 16.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 82249-69-2
References:
1. Fukuda, H., Iwade, S. and Kimura, A. A new enzyme: long acyl aminoacylase from Pseudomonas diminuta. J. Biochem. (Tokyo) 91 (1982) 1731-1738. [PMID: 7096313]
Accepted name: N,N-dimethylformamidase
Reaction: N,N-dimethylformamide + H2O = dimethylamine + formate
Other name(s): dimethylformamidase; DMFase
Systematic name: N,N-dimethylformamide amidohydrolase
Comments: An iron protein. Also acts on N-ethylformamide and N-methyl-formamide and, more slowly, on N,N-diethylformamide, N,N-dimethylacetamide and unsubstituted acyl amides.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 104645-73-0
References:
1. Schär, H.-P., Holzmann, W., Ramos Tombo, G.M. and Ghisalba, O. Purification and characterization of N,N-dimethylformamidase from Pseudomonas DMF 3/3. Eur. J. Biochem. 158 (1986) 469-475. [PMID: 3732281]
Accepted name: tryptophanamidase
Reaction: L-tryptophanamide + H2O = L-tryptophan + NH3
Other name(s): tryptophan aminopeptidase; L-tryptophan aminopeptidase
Systematic name: L-tryptophanamide amidohydrolase
Comments: Requires Mn2+. Also acts on N-ethylformamide and L-tyrosinamide, and on some tryptophan dipeptides.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 76689-19-5
References:
1. Iwayama, A., Kimura, T., Adachi, O. and Ameyama, M. Crystallization and characterization of a novel aminopeptidase from Trichosporon cutaneum. Agric. Biol. Chem. 47 (1983) 2483-2493.
Accepted name: N-benzyloxycarbonylglycine hydrolase
Reaction: N-benzyloxycarbonylglycine + H2O = benzyl alcohol + CO2 + glycine
Other name(s): benzyloxycarbonylglycine hydrolase; Nα-carbobenzoxyamino acid amidohydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase I
Systematic name: N-benzyloxycarbonylglycine urethanehydrolase
Comments: Also acts, more slowly, on N-benzyloxycarbonylalanine, but not on the corresponding derivatives of other amino acids or on N-benzyloxycarbonylpeptides. Requires Co2+ or Zn2+. cf. EC 3.5.1.64 Nα-benzyloxycarbonylleucine hydrolase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 91930-69-7
References:
1. Murao, S., Matsumura, E. and Kawano, T. Isolation and characterization of a novel enzyme, Nα-benzyloxycarbonyl amino acid urethane hydrolase, from Streptococcus faecalis R ATCC 8043. Agric. Biol. Chem. 49 (1985) 967-972.
Accepted name: N-carbamoylsarcosine amidase
Reaction: N-carbamoylsarcosine + H2O = sarcosine + CO2 + NH3
For diagram of reaction click here.
Other name(s): carbamoylsarcosine amidase
Systematic name: N-carbamoylsarcosine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 92767-52-7
References:
1. Deeg, R., Roeder, A., Siedel, J., Gauhl, H. and Ziegenhorn, J. Process and reagent for the determination of N-carbamoylsarcosine with the use of a new enzyme. Patent DE3248145, 1982, Chem. Abstr. 101 (1984) 187515.
Accepted name: N-(long-chain-acyl)ethanolamine deacylase
Reaction: N-(long-chain-acyl)ethanolamine + H2O = a long-chain carboxylate + ethanolamine
Other name(s): N-acylethanolamine amidohydrolase; acylethanolamine amidase
Systematic name: N-(long-chain-acyl)ethanolamine amidohydrolase
Comments: Does not act on N-acylsphingosine or N,O-diacylethanolamine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 99283-61-1
References:
1. Schmid, P.C., Zuzarte-Augustin, M.L. and Schmid, H.H.O. Properties of rat liver N-acylethanolamine amidohydrolase. J. Biol. Chem. 260 (1985) 14145-14149. [PMID: 4055775]
Accepted name: mimosinase
Reaction: (S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H2O = 3-hydroxy-4H-pyrid-4-one + L-serine
Systematic name: mimosine amidohydrolase
Comments: An enzyme from Leucaena leucocephala leaf, which also contains the toxic amino acid, mimosine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 104118-49-2
References:
1. Tangendjaja, B., Lowry, J.B. and Wills, R.H. Isolation of a mimosine degrading enzyme from Leucaena leaf. J. Sci. Food Agric. 37 (1986) 523-526.
Accepted name: acetylputrescine deacetylase
Reaction: N-acetylputrescine + H2O = acetate + putrescine
Glossary: spermidine
Systematic name: N-acetylputrescine acetylhydrolase
Comments: The enzyme from Micrococcus luteus also acts on N8-acetylspermidine and acetylcadaverine, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 103679-48-7
References:
1. Suzuki, O., Ishikawa, Y., Miyazaki, K., Izu, K. and Matsumoto, T. Acetylputrescine deacetylase from Micrococcus luteus K-11. Biochim. Biophys. Acta 882 (1986) 140-142.
Accepted name: 4-acetamidobutyrate deacetylase
Reaction: 4-acetamidobutanoate + H2O = acetate + 4-aminobutanoate
Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA
Systematic name: 4-acetamidobutanoate amidohydrolase
Comments: Also acts on N-acetyl-β-alanine and 5-acetamidopentanoate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 102347-82-0
References:
1. Haywood, G.W. and Large, P.J. 4-Acetamidobutyrate deacetylase in the yeast Candida boidinii grown on putrescine or spermidine as sole nitrogen source and its probable role in polyamine catabolism. J. Gen. Microbiol. 132 (1986) 7-14.
Accepted name: Nα-benzyloxycarbonylleucine hydrolase
Reaction: Nα-benzyloxycarbonyl-L-leucine + H2O = benzyl alcohol + CO2 + L-leucine
Other name(s): benzyloxycarbonylleucine hydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase IV
Systematic name: Nα-benzyloxycarbonyl-L-leucine urethanehydrolase
Comments: Also acts on Nα-t-butoxycarbonyl-L-leucine, and, more slowly, on the corresponding derivatives of L-aspartate, L-methionine, L-glutamate and L-alanine. cf. EC 3.5.1.58 N-benzyloxycarbonylglycine hydrolase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 100630-47-5
References:
1. Matsumura, E., Shin, T., Murao, S., Sakaguchi, M. and Kawano, T. A novel enzyme, Nα-benzyloxycarbonyl amino acid urethane hydrolase IV. Agric. Biol. Chem. 49 (1985) 3643-3645.
Accepted name: theanine hydrolase
Reaction: N5-ethyl-L-glutamine + H2O = L-glutamate + ethylamine
Glossary: L-theanine = N5-ethyl-L-glutamine
Systematic name: N5-ethyl-L-glutamine amidohydrolase
Comments: Also acts on other N-alkyl-L-glutamines.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 99533-51-4
References:
1. Tsushida, T. and Takeo, T. An enzyme hydrolyzing L-theanine in tea leaves. Agric. Biol. Chem. 49 (1985) 2913-2917.
Accepted name: 2-(hydroxymethyl)-3-(acetamidomethylene)succinate hydrolase
Reaction: 2-(hydroxymethyl)-3-(acetamidomethylene)succinate + 2 H2O = acetate + 2-(hydroxymethyl)-4-oxobutanoate + NH3 + CO2
Other name(s): compound B hydrolase; α-hydroxymethyl-α'-(N-acetylaminomethylene)succinic acid hydrolase
Systematic name: 2-(hydroxymethyl)-3-(acetamidomethylene)succinate amidohydrolase (deaminating, decarboxylating)
Comments: Involved in the degradation of pyridoxin by Pseudomonas and Arthrobacter.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 95829-26-8
References:
1. Huynh, M.S. and Snell, E.E. Enzymes of vitamin B6 degradation. Purification and properties of two N-acetylamidohydrolases. J. Biol. Chem. 260 (1985) 2379-2383. [PMID: 3972793]
Accepted name: 4-methyleneglutaminase
Reaction: 4-methylene-L-glutamine + H2O = 4-methylene-L-glutamate + NH3
Other name(s): 4-methyleneglutamine deamidase; 4-methyleneglutamine amidohydrolase
Systematic name: 4-methylene-L-glutamine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 86855-36-9
References:
1. Ibrahim, S.A., Lea, P.J. and Fowden, L. Preparation and properties of 4-methyleneglutaminase from the leaves of peanut (Arachis hypogaea). Phytochemistry 23 (1984) 1545-1549.
Accepted name: N-formylglutamate deformylase
Reaction: N-formyl-L-glutamate + H2O = formate + L-glutamate
For diagram click here.
Other name(s): β-citryl-L-glutamate hydrolase; formylglutamate deformylase; N-formylglutamate hydrolase; β-citrylglutamate amidase; β-citryl-L-glutamate amidohydrolase; β-citryl-L-glutamate amidase; β-citrylglutamate amidase; β-citryl-L-glutamate-hydrolyzing enzyme
Systematic name: N-formyl-L-glutamate amidohydrolase
Comments: The animal enzyme also acts on β-citryl-L-glutamate and β-citryl-L-glutamine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 97286-12-9
References:
1. Hu, L., Mulfinger, L.M. and Phillips, A.T. Purification and properties of formylglutamate amidohydrolase from Pseudomonas putida. J. Bacteriol. 169 (1987) 4696-4702. [PMID: 3308850]
2. Miyake, M., Innami, T. and Kakimoto, Y. A β-citryl-L-glutamate-hydrolysing enzyme in rat testes. Biochim. Biophys. Acta 760 (1983) 206-214. [PMID: 6414521]
Accepted name: glycosphingolipid deacylase
Reaction: Hydrolysis of gangliosides and neutral glycosphingolipids, releasing fatty acids to form the lyso-derivatives
Other name(s): glycosphingolipid ceramide deacylase
Systematic name: glycosphingolipid amidohydrolase
Comments: Does not act on sphingolipids such as ceramide. Not identical with EC 3.5.1.23 ceramidase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 122544-53-0
References:
1. Hirabayashi, Y., Kimura, M., Matsumoto, M., Yamamoto, K., Kadowaki, S. and Tochikura, T. A novel glycosphingolipid hydrolyzing enzyme, glycosphingolipid ceramide deacylase, which cleaves the linkage between the fatty acid and sphingosine base in glycosphingolipids. J. Biochem. (Tokyo) 103 (1988) 1-4. [PMID: 3360750]
Accepted name: aculeacin-A deacylase
Reaction: Hydrolysis of the amide bond in aculeacin A and related neutral lipopeptide antibiotics, releasing the long-chain fatty acid side-chain
Other name(s): aculeacin A acylase
Systematic name: aculeacin-A amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 121479-50-3
References:
1. Takeshima, H., Inokoshi, J., Takada, Y., Tanaka, H. and Omura, S. A deacylation enzyme for aculeacin A, a neutral lipopeptide antibiotic, from Actinoplanes utahensis: purification and characterization. J. Biochem. (Tokyo) 105 (1989) 606-610. [PMID: 2760018]
Accepted name: N-feruloylglycine deacylase
Reaction: N-feruloylglycine + H2O = ferulate + glycine
Other name(s): N-feruloylglycine hydrolase
Systematic name: N-feruloylglycine amidohydrolase
Comments: Hydrolyses a range of L-amino acids from the cinnamoyl and substituted cinnamoyl series. Not identical with EC 3.5.1.14 aminoacylase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 118731-84-3
References:
1. Martens, M., Cottenie-Ruysschaert, M., Hanselaer, R., De Cooman, L., CASteele, K.V. and Van Sumere, F. N-Feruloylglycine amidohydrolase from barley seeds and isolated barley embryos. Phytochemistry 27 (1988) 2457-2463.
2. Martens, M., Cottenie-Ruysschaert, M., Hanselaer, R., De Cooman, L., CASteele, K.V. and Van Sumere, F. Characteristics and specificity of purified N-feruloylglycine amidohydrolase from isolated barley embryos. Phytochemistry 27 (1988) 2465-2475.
Accepted name: D-benzoylarginine-4-nitroanilide amidase
Reaction: N-benzoyl-D-arginine-4-nitroanilide + H2O = N-benzoyl-D-arginine + 4-nitroaniline
Other name(s): benzoyl-D-arginine arylamidase; D-BAPA-ase
Systematic name: N-benzoyl-D-arginine-4-nitroanilide amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 119345-26-5
References:
1. Gofshtein-Gandman, L.V., Keynan, A. and Milner, Y. Bacteria of the genus Bacillus have a hydrolase stereospecific to the D isomer of benzoyl-arginine-p-nitroanilide. J. Bacteriol. 170 (1988) 5895-5900. [PMID: 3142860]
Accepted name: carnitinamidase
Reaction: L-carnitinamide + H2O = L-carnitine + NH3
Other name(s): L-carnitinamidase; carnitine amidase; L-carnitine amidase
Systematic name: L-carnitinamide amidohydrolase
Comments: Does not act on D-carnitinamide.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 117444-04-9
References:
1. Nakayama, K., Honda, H., Ogawa, Y., Ozawa, T. and Ota, T. Method for producing carnitine, L-carnitinamide hydrolase and method for producing same. Patent DE3728321, 1988, Chem. Abstr. 109 (1988) 228738.
Accepted name: chenodeoxycholoyltaurine hydrolase
Reaction: chenodeoxycholoyltaurine + H2O = chenodeoxycholate + taurine
Glossary: chenodeoxycholate = 3α,7α-dihydroxy-5β-cholan-24-oate
Systematic name: chenodeoxycholoyltaurine amidohydrolase
Comments: Some other taurine conjugates are hydrolysed, but not glycine conjugates of bile acids.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 125752-75-2
References:
1. Kawamoto, K., Horibe, I. and Uchida, K. Purification and characterization of a new hydrolase for conjugated bile acids, chenodeoxycholyltaurine hydrolase, from Bacteroides vulgatus. J. Biochem. (Tokyo) 106 (1989) 1049-1053. [PMID: 2628421]
Accepted name: urethanase
Reaction: urethane + H2O = ethanol + CO2 + NH3
Other name(s): urethane hydrolase
Systematic name: urethane amidohydrolase (decarboxylating)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 122007-70-9
References:
1. Kobashi, K., Takebe, S. and Sakai, T. Urethane-hydrolyzing enzyme from Citrobacter sp. Chem. Pharm. Bull. 38 (1990) 1326-1328. [PMID: 2393957]
Accepted name: arylalkyl acylamidase
Reaction: N-acetylarylalkylamine + H2O = arylalkylamine + acetate
Other name(s): aralkyl acylamidase
Systematic name: N-acetylarylalkylamine amidohydrolase
Comments: identified in Pseudomonas putida. Strict specificity for N-acetyl arylalkylamines, including N-acetyl-2-phenylethylamine, N-acetyl-3-phenylpropylamine, N-acetyldopamine, N-acetyl-serotonin and melatonin. It also accepts arylalkyl acetates but not acetanilide derivatives, which are common substrates of EC 3.5.1.13, aryl acylamidase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Shimizu, S., Ogawa, J., Chung, M.C.-M., Yamada, H. Purification and characterization of a novel enzyme, arylalkyl acylamidase, from Pseudomonas putida Sc2. Eur. J. Biochem. 209 (1992) 375-382. [PMID: 1396711]
Accepted name: N-carbamoyl-D-amino-acid hydrolase
Reaction: an N-carbamoyl-D-amino acid + H2O = a D-amino acid + NH3 + CO2
Other name(s): D-N-carbamoylase; N-carbamoylase (ambiguous); N-carbamoyl-D-amino acid hydrolase
Systematic name: N-carbamoyl-D-amino-acid amidohydrolase
Comments: This enzyme, along with EC 3.5.1.87 (N-carbamoyl-L-amino-acid hydrolase), EC 5.1.99.5 (hydantoin racemase) and hydantoinase, forms part of the reaction cascade known as the "hydantoinase process", which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids [2]. It has strict stereospecificity for N-carbamoyl-D-amino acids and does not act upon the corresponding L-amino acids or on the N-formyl amino acids, N-carbamoyl-sarcosine, -citrulline, -allantoin and -ureidopropanoate, which are substrates for other amidohydrolases.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 71768-08-6
References:
1. Ogawa, J., Shimizu, S., Yamada, H. N-Carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c; purification and characterization. Eur. J. Biochem. 212 (1993) 685-691. [PMID: 8462543]
2. Altenbuchner, J., Siemann-Herzberg, M. and Syldatk, C. Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids. Curr. Opin. Biotechnol. 12 (2001) 559-563. [PMID: 11849938]
Accepted name: glutathionylspermidine amidase
Reaction: glutathionylspermidine + H2O = glutathione + spermidine
Glossary: spermidine
Other name(s): glutathionylspermidine amidohydrolase (spermidine-forming)
Systematic name: γ-L-glutamyl-L-cysteinyl-glycine:spermidine amidase
Comments: spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine synthase (EC 6.3.1.8) reaction, resulting in a net hydrolysis of ATP.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 171040-71-4
References:
1. Bollinger, J.M., Kwon, D.S., Huisman, G.W., Kolter, R., Walsh, C.T. Glutathionylspermidine metabolism in E. coli. Purification, cloning, overproduction and characterization of a bifunctional glutathionylspermidine synthetase/amidase. J. Biol. Chem. 270 (1995) 14031-14041. [PMID: 7775463]
Accepted name: phthalyl amidase
Reaction: a phthalylamide + H2O = phthalic acid + a substituted amine
Systematic name: phthalyl-amide amidohydrolase
Comments: in the entry, "phthalyl" is used to mean "2-carboxybenzoyl". The enzyme from Xanthobacter agilis hydrolyses phthalylated amino acids, peptides, β-lactams, aromatic and aliphatic amines. The substituent on nitrogen may be an alkyl group, but may also be complex, giving an amino acid or peptide derivative. Substitutions on the phthalyl ring include 6-F, 6-NH2, 3-OH, and a nitrogen in the aromatic ring ortho to the carboxy group attached to the amine. No cofactors are required
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 169150-79-2
References:
1. Briggs, B.S., Kreuzman, A.J., Whitesitt, C., Yeh, W.K., Zmijewski, M. Discovery, purification, and properties of o-phthalyl amidase from Xanthobacter agilis. J. Mol. Catal., B Enzym. 2 (1996) 53-69.
2. Black, T.D., Briggs, B.S., Evans, R., Muth, W.L., Vangala, S., Zmijewski, M.J. o-Phthalyl amidase in the synthesis of Loracarbef: process development using this novel biocatalyst. Biotechnol. Lett. 18 (1996) 875-880.
3. Costello, C., Kreuzman, A., Zmijewski, M. Selective deprotection of phthalyl protected proteins. Tetrahedron Lett. 37 (1996) 7469-7472.
4. Briggs, B.S., Zmijewski, M.J. Enzyme from microbial source: phthalyl amidase. Patent US5445959, 1995. Chem. Abstr. 123 (1995) 250104 (PDF).
[EC 3.5.1.80 Deleted entry: identical to EC 3.5.1.25, N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.80 created 1999, deleted 2002)]
Accepted name: N-acyl-D-amino-acid deacylase
Reaction: N-acyl-D-amino acid + H2O = a carboxylate + D-amino acid
Systematic name: N-acyl-D-amino acid amidohydrolase
Comments: The enzyme from Alcaligenes denitrificans subsp. xylosoxydans and Alcaligenes xylosoxydans subsp. xylosoxydans has wide specificity; hydrolyses N-acyl derivative of neutral D-amino acids. Used in separating D- and L-amino acids. Requires zinc.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 65979-42-2
References:
1. Wakayama, M., Katsuno, Y., Hayashi, S., Miyamoto, Y., Sakai, K. and Moriguchi, M. Cloning and sequencing of a gene encoding D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 and expression of the gene in Escherichia coli. Biosci. Biotechnol. Biochem. 59 (1995) 2115-2119. [PMID: 8541651]
2. Wakayama, M., Hayashi, S., Yatsuda, Y., Katsuno, Y., Sakai, K. and Moriguchi, M. Overproduction of D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 in Escherichia coli and its purification. Protein Expr. Purif. 7 (1996) 395-399. [PMID: 8776758]
Accepted name: N-acyl-D-glutamate deacylase
Reaction: N-acyl-D-glutamate + H2O = a carboxylate + D-glutamate
Systematic name: N-acyl-D-glutamate amidohydrolase
Comments: the enzyme from Alcaligenes xylosoxydans subsp. xylosoxydans and Pseudomonas sp. is specific for N-acyl-D-glutamate. Requires zinc.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 82249-69-2
References:
1. Wakayama, M., Ahshika, T., Miyamoto, Y., Yoshikawa, T., Sonoda, Y., Sakai, K. and Moriguchi, M. Primary structure of N-acyl-D-glutamate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6. J. Biochem. (Tokyo) 118 (1995) 204-209. [PMID: 8537313]
2. Wakayama, M., Miura, Y., Oshima, K., Sakai, K. and Moriguchi, M. Metal-characterization of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. strain 5f-1. Biosci. Biotechnol. Biochem. 59 (1995) 1489-1492. [PMID: 7549100]
3. Wakayama, M., Tsutsumi, T., Yada, H., Sakai, K. and Moriguchi, M. Chemical modification of histidine residue of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. 5f-1. Biosci. Biotechnol. Biochem. 60 (1996) 650-653. [PMID: 8829533]
Accepted name: N-acyl-D-aspartate deacylase
Reaction: N-acyl-D-aspartate + H2O = a carboxylate + D-aspartate
Systematic name: N-acyl-D-aspartate amidohydrolase
Comments: the enzyme from Alcaligenes xylosoxydans subsp. xylosoxydans is specific for N-acyl-D-aspartate. Requires zinc.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9031-86-1
References:
1. Moriguchi, M., Sakai, K., Katsuno, Y., Maki, T., Wakayama, M. Purification and characterization of novel N-acyl-D-aspartate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6. Biosci. Biotechnol. Biochem. 57 (1993) 1145-1148. [PMID: 7763985]
2. Wakayama, M., Watanabe, E., Takenaka, Y., Miyamoto, Y., Tau, Y., Sakai, K., Moriguchi, M. Cloning, expression and nucleotide sequence of the N-acyl-D-aspartate amidohydrolase gene from Alcaligenes xylosoxydans subsp. xylosoxydans A-6. J. Ferment. Bioeng. 80 (1995) 311-317.
Accepted name: biuret amidohydrolase
Reaction: biuret + H2O = urea-1-carboxylate + NH3
Glossary: biuret = imidodicarbonic diamide
allophanate = urea-1-carboxylate
Systematic name: biuret amidohydrolase
Comments: Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) and EC 3.5.1.54 (allophanate hydrolase), this enzyme forms part of the cyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria. Urea-1-carboxylate rather than urea (as was thought previously) is the 2-nitrogen intermediate in cyanuric-acid metabolism in bacteria [2]. The product, urea-1-carboxylate, can spontaneously decarboxylate under acidic conditions to form urea but, under physiological conditions, it can be converted into CO2 and ammonia by the action of EC 3.5.1.54 [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD CAS registry number:
References:
1. Cook, A.M., Beilstein, P., Grossenbacher, H. and Hutter, R. Ring cleavage and degradative pathway of cyanuric acid in bacteria. Biochem. J. 231 (1985) 25-30. [PMID: 3904735]
2. Cheng, G., Shapir, N., Sadowsky, M.J. and Wackett, L.P. Allophanate hydrolase, not urease, functions in bacterial cyanuric acid metabolism. Appl. Environ. Microbiol. 71 (2005) 4437-4445. [PMID: 16085834]
3. Shapir, N., Sadowsky, M.J. and Wackett, L.P. Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP. J. Bacteriol. 187 (2005) 3731-3738. [PMID: 15901697]
Accepted name: (S)-N-acetyl-1-phenylethylamine hydrolase
Reaction: N-acetylphenylethylamine + H2O = phenylethylamine + acetate
Other name: (S)-N-acetyl-1-phenylethylamine amidohydrolase
Systematic name: (S)-N-acetylphenylethylamine:H2O hydrolase
Comments: Inhibited by phenylmethanesulfonyl fluoride. Some related acetylated compounds are hydrolysed with variable enantiomeric selectivities.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 192230-94-7
References:
1. Brunella, A., Graf, M., Kittelmann, M., Lauma, K. and Ghisalba, O. Production, purification, and characterization of a highly enantioselective (S)-N-acetyl-1-phenylethyl amidohydrolase from Rhodococcus. Appl. Microbiol. Biotechnol. 47 (1997) 515-520.
Accepted name: mandelamide amidase
Reaction: (R)-mandelamide + H2O = (R)-mandelate + NH3
Glossary: (R)-mandelate = (R)-2-hydroxy-2-phenylacetate
Other name(s): Pseudomonas mandelamide hydrolase
Systematic name: mandelamide hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yamamoto, K., Oishi, K., Fujimatsu, I. and Komatsu, K. Production of R-(–)-mandelic acid from mandelonitrile by Alcaligenes faecalis ATCC 8750. Appl. Environ. Microbiol. 57 (1991) 3028-3032. [PMID: 1660699]
Accepted name: N-carbamoyl-L-amino-acid hydrolase
Reaction: an N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H2O = an L-2-amino acid + NH3 + CO2
Other name(s): N-carbamyl L-amino acid amidohydrolase; N-carbamoyl-L-amino acid amidohydrolase; L-N-carbamoylase; N-carbamoylase (ambiguous)
Systematic name: N-carbamoyl-L-amino-acid amidohydrolase
Comments: This enzyme, along with EC 3.5.1.77 (N-carbamoyl-D-amino-acid hydrolase), EC 5.1.99.5 (hydantoin racemase) and hydantoinase, forms part of the reaction cascade known as the "hydantoinase process", which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids [3]. The enzyme from Alcaligenes xylosoxidans has broad specificity for carbamoyl-L-amino acids, although it is inactive on the carbamoyl derivatives of glutamate, aspartate, arginine, tyrosine or tryptophan. The enzyme from Sinorhizobium meliloti requires a divalent cation for activity and can hydrolyse N-carbamoyl-L-tryptophan as well as N-carbamoyl L-amino acids with aliphatic substituents [2]. The enzyme is inactive on derivatives of D-amino acids. In addition to N-carbamoyl L-amino acids, the enzyme can also hydrolyse formyl and acetyl derivatives to varying degrees [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Ogawa, J., Miyake, H. and Shimizu, S. Purification and characterization of N-carbamoyl-L-amino acid amidohydrolase with broad substrate specificity from Alcaligenes xylosoxidans. Appl. Microbiol. Biotechnol. 43 (1995) 1039-1043. [PMID: 8590654]
2. Martínez-Rodríguez, S., Clemente-Jiménez, J.M., Rodríguez-Vico, F. and Las Heras-Vázquez, F.J. Molecular cloning and biochemical characterization of L-N-carbamoylase from Sinorhizobium meliloti CECT4114. J. Mol. Microbiol. Biotechnol. 9 (2005) 16-25. [PMID: 16254442]
3. Altenbuchner, J., Siemann-Herzberg, M. and Syldatk, C. Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids. Curr. Opin. Biotechnol. 12 (2001) 559-563. [PMID: 11849938]
Accepted name: peptide deformylase
Reaction: formyl-L-methionyl peptide + H2O = formate + methionyl peptide
Systematic name: formyl-L-methionyl peptide amidohydrolase
Comments: Requires Fe(II). Also requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Differs in substrate specifity from EC 3.5.1.27 (N-formylmethionylaminoacyl-tRNA deformylase) and EC 3.5.1.31 (formylmethionine deformylase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 369636-51-1
References:
1. Adams, J.M. On the release of the formyl group from nascent protein. J. Mol. Biol. 33 (1968) 571-589. [PMID: 4973445]
2. Mazel, D., Pochet, S. and Marliere, P. Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation. EMBO J. 13 (1994) 914-923. [PMID: 8112305]
3. Chan, M.K., Gong, W., Rajagopalan, P.T.R., Hao, B., Tsai, C.M. and Pei, D. Crystal structure of the Escherichia coli peptide deformylase. Biochemistry 36 (1997) 13904-13909. [PMID: 9374869]
4. Becker, A., Schlichting, I., Kabsch, W., Schultz, S. and Wagner, A.F.V. Structure of peptide deformylase and identification of the substrate binding site. J. Biol. Chem. 273 (1998) 11413-11416. [PMID: 9565550]
5. Becker, A., Schlichting, I., Kabsch, W., Groche, D., Schultz, S. and Wagner, A.F. Iron center, substrate recognition, and mechanism of peptide deformylase. Nat. Struct. Biol. 5 (1998) 1053-1058. [PMID: 9846875]
6. Rajagopalan, P.T.R., Yu, X.C. and Pei, D. Peptide deformylase: a new type of mononuclear iron protein. J. Am. Chem. Soc. 119 (1997) 12418-12419.
7. Groche, D., Becker, A., Schlichting, I., Kabsch, W., Schultz, S. and Wagner, A.F.V. Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site. Biochem. Biophys. Res. Commun. 246 (1998) 342-346. [PMID: 9610360]
8. Rajagopalan, P.T.R., Grimme, S. and Pei, D. Characterization of cobalt(II)-substituted peptide deformylase: function of the metal ion and the catalytic residue Glu-133. Biochemistry 39 (2000) 779-790. [PMID: 10651644]
9. Hu, Y.J., Wei, Y., Zhou, Y., Rajagopalan, P.T.R. and Pei, D. Determination of substrate specificity for peptide deformylase through the screening of a combinatorial peptide library. Biochemistry 38 (1999) 643-650. [PMID: 9888804]
10. Ragasu, S., Mouchet, P., Lazennec, C., Dive, V. and Meinnel, T. Substrate recognition and selectivity of peptide deformylase. Similarities and differences with metzincins and thermolysin. J. Mol. Biol. 289 (1999) 1445-1457. [PMID: 10373378]
11. Giglione, C., Pierre, M. and Meinnel, T. Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents. Mol. Microbiol. 36 (2000) 1197-1205. [PMID: 10931273]
12. Pei, D. Peptide deformylase: a target for novel antibiotics? Emerging Therapeutic Targets 5 (2001) 23-40.
Accepted name: N-acetylglucosaminylphosphatidylinositol deacetylase
Reaction: 6-(N-acetyl-α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
For diagram click here.
Other name(s): N-acetyl-D-glucosaminylphosphatidylinositol acetylhydrolase; N-acetylglucosaminylphosphatidylinositol de-N-acetylase; GlcNAc-PI de-N-acetylase; GlcNAc-PI deacetylase; acetylglucosaminylphosphatidylinositol deacetylase
Systematic name: 6-(N-acetyl-α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol acetylhydrolase
Comments: Involved in the second step of glycosylphosphatidylinositol (GPI) anchor formation in all eukaryotes. The enzyme appears to be composed of a single subunit (PIG-L in mammalian cells and GPI12 in yeast). In some species, the long-chain sn-1-acyl group of the phosphatidyl group is replaced by a long-chain alkyl or alk-1-enyl group.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 122191-30-4
References:
1. Doering, T.L., Masteron, W.J., Englund, P.T. and Hart, G.W. Biosynthesis of the glycosyl phosphatidylinositol membrane anchor of the trypanosome variant surface glycoprotein. Origin of the non-acetylated glucosamine. J. Biol. Chem. 264 (1989) 11168-11173. [PMID: 2525555]
2. Nakamura, N., Inoue, N., Watanabe, R., Takahashi, M., Takeda, J., Stevens, V.L. and Kinoshita, T. Expression cloning of PIG-L, a candidate N-acetylglucosaminyl-phosphatidylinositol deacetylase. J. Biol. Chem. 272 (1997) 15834-15840. [PMID: 9188481]
3. Watanabe, R., Ohishi, K., Maeda, Y., Nakamura, N. and Kinoshita, T. Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis. Biochem. J. 339 (1999) 185-192. [PMID: 10085243]
4. Smith, T.K, Crossman, A., Borissow, C.N., Paterson, M.J., Dix, A., Brimacombe, J.S. and Ferguson, M.A.J. Specificity of GlcNAc-PI de-N-acetylase of GPI biosynthesis and synthesis of parasite-specific suicide substrate inhibitors. EMBO J. 20 (2001) 3322-3332. [PMID: 11432820]
Accepted name: adenosylcobinamide hydrolase
Reaction: adenosylcobinamide + H2O = adenosylcobyric acid + (R)-1-aminopropan-2-ol
For diagram click here.
Other name(s): CbiZ; AdoCbi amidohydrolase
Systematic name: adenosylcobinamide amidohydrolase
Comments: Involved in the salvage pathway of cobinamide in archaea. Archaea convert adenosylcobinamide (AdoCbi) into adenosylcobinamide phosphate (AdoCbi-P) in two steps. First, the amidohydrolase activity of CbiZ cleaves off the aminopropanol moiety of AdoCbi yielding adenosylcobyric acid (AdoCby); second, AdoCby is converted into AdoCbi-P by the action of EC 6.3.1.10, adenosylcobinamide-phosphate synthase (CbiB).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 905988-16-1
References:
1. Woodson, J.D. and Escalante-Semerena, J.C. CbiZ, an amidohydrolase enzyme required for salvaging the coenzyme B12 precursor cobinamide in archaea. Proc. Natl. Acad. Sci. USA 101 (2004) 3591-3596. [PMID: 14990804]
Accepted name: N-substituted formamide deformylase
Reaction: N-benzylformamide + H2O = formate + benzylamine
For diagram click here.
Other name(s): NfdA
Systematic name: N-benzylformamide amidohydrolase
Comments: Zinc is a cofactor. While N-benzylformamide is the best substrate, the enzyme from Arthrobacter pascens can also act on the N-substituted formamides N-butylformamide, N-allylformamide, N-[2-(cyclohex-1-enyl)ethyl]formamide and N-(1-phenylethyl)formamide, but much more slowly. Amides of other acids do not act as substrates.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 115299-95-1
References:
1. Fukatsu, H., Hashimoto, Y., Goda, M., Higashibata, H. and Kobayashi, M. Amine-synthesizing enzyme N-substituted formamide deformylase: screening, purification, characterization, and gene cloning. Proc. Natl. Acad. Sci. USA 101 (2004) 13726-13731. [PMID: 15358859]
Accepted name: pantetheine hydrolase
Reaction: (R)-pantetheine + H2O = (R)-pantothenate + 2-aminoethanethiol
Other name(s): pantetheinase; vanin; vanin-1
Systematic name: (R)-pantetheine amidohydrolase
Comments: The enzyme hydrolyses only one of the amide bonds of pantetheine. The substrate analogues phosphopantetheine and CoA are not substrates. The enzyme recycles pantothenate (vitamin B5) and produces 2-aminoethanethiol, a potent anti-oxidant [5].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 56093-18-6
References:
1. Duprè, S. and Cavallini, D. Purification and properties of pantetheinase from horse kidney. Methods Enzymol. 62 (1979) 262-267. [PMID: 440106]
2. Duprè, S., Chiaraluce, R., Nardini, M., Cannella, C., Ricci, G. and Cavallini, D. Continuous spectrophotometric assay of pantetheinase activity. Anal. Biochem. 142 (1984) 175-181. [PMID: 6549111]
3. Maras, B., Barra, D., Duprè, S. and Pitari, G. Is pantetheinase the actual identity of mouse and human vanin-1 proteins? FEBS Lett. 461 (1999) 149-152. [PMID: 10567687]
4. Aurrand-Lions, M., Galland, F., Bazin, H., Zakharyev, V.M., Imhof, B.A. and Naquet, P. Vanin-1, a novel GPI-linked perivascular molecule involved in thymus homing. Immunity 5 (1996) 391-405. [PMID: 8934567]
5. Pitari, G., Malergue, F., Martin, F., Philippe, J.M., Massucci, M.T., Chabret, C., Maras, B., Dupre, S., Naquet, P. and Galland, F. Pantetheinase activity of membrane-bound vanin-1: lack of free cysteamine in tissues of Vanin-1 deficient mice. FEBS Lett. 483 (2000) 149-154. [PMID: 11042271]
6. Martin, F., Malergue, F., Pitari, G., Philippe, J.M., Philips, S., Chabret, C., Granjeaud, S., Mattei, M.G., Mungall, A.J., Naquet, P. and Galland, F. Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and encode isoforms of pantetheinase ectoenzymes. Immunogenetics 53 (2001) 296-306. [PMID: 11491533]
7. Pace, H.C. and Brenner, C. The nitrilase superfamily: classification, structure and function. Genome Biol. 2 (2001) 0001.1-001.9. [PMID: 11380987]
Accepted name: glutaryl-7-aminocephalosporanic-acid acylase
Reaction: (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate
For diagram click here.
Other name(s): 7β-(4-carboxybutanamido)cephalosporanic acid acylase; cephalosporin C acylase; glutaryl-7-ACA acylase; CA; GCA; GA; cephalosporin acylase; glutaryl-7-aminocephalosporanic acid acylase; GL-7-ACA acylase
Systematic name: (7R)-7-(4-carboxybutanamido)cephalosporanate amidohydrolase
Comments: Forms 7-aminocephalosporanic acid, a key intermediate in the synthesis of cephem antibiotics. It reacts only weakly with cephalosporin C.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 56645-46-6
References:
1. Ishii, Y., Saito, Y., Fujimura, T., Sasaki, H., Noguchi, Y., Yamada, H., Niwa, M. and Shimomura, K. High-level production, chemical modification and site-directed mutagenesis of a cephalosporin C acylase from Pseudomonas strain N176. Eur. J. Biochem. 230 (1995) 773-778. [PMID: 7607251]
2. Kinoshita, T., Tada, T., Saito, Y., Ishii, Y., Sato, A. and Murata, M. Crystallization and preliminary X-ray analysis of cephalosporin C acylase from Pseudomonas sp. strain N176. Acta Crystallogr. D Biol. Crystallogr. 56 (2000) 458-459. [PMID: 10739919]
3. Monti, D., Carrea, G., Riva, S., Baldaro, E. and Frare, G. Characterization of an industrial biocatalyst: immobilized glutaryl-7-ACA acylase. Biotechnol. Bioeng. 70 (2000) 239-244. [PMID: 10972935]
4. Kwon, T.H., Rhee, S., Lee, Y.S., Park, S.S. and Kim, K.H. Crystallization and preliminary X-ray diffraction analysis of glutaryl-7-aminocephalosporanic acid acylase from Pseudomonas sp. GK16. J. Struct. Biol. 131 (2000) 79-81. [PMID: 10945972]
5. Kim, Y., Yoon, K.-H., Khang, Y., Turley, S. and Hol, W.G.J. The 2.0 Å crystal structure of cephalosporin acylase. Structure Fold Des. 8 (2000) 1059-1068. [PMID: 11080627]
6. Huang, X., Zeng, R., Ding, X., Mao, X., Ding, Y., Rao, Z., Xie, Y., Jiang, W. and Zhao, G. Affinity alkylation of the Trp-B4 residue of the β-subunit of the glutaryl 7-aminocephalosporanic acid acylase of Pseudomonas sp. 130. J. Biol. Chem. 277 (2002) 10256-10264. [PMID: 11782466]
7. Kim, J.K., Yang, I.S., Rhee, S., Dauter, Z., Lee, Y.S., Park, S.S. and Kim, K.H. Crystal structures of glutaryl 7-aminocephalosporanic acid acylase: insight into autoproteolytic activation. Biochemistry 42 (2003) 4084-4093. [PMID: 12680762]
Accepted name: γ-glutamyl-γ-aminobutyrate hydrolase
Reaction: 4-(L-γ-glutamylamino)butanoate + H2O = 4-aminobutanoate + L-glutamate
Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA
Other name(s): γ-glutamyl-GABA hydrolase; PuuD; YcjL; 4-(γ-glutamylamino)butanoate amidohydrolase
Systematic name: 4-(L-γ-glutamylamino)butanoate amidohydrolase
Comments: Forms part of a putrescine-utilizing pathway in Escherichia coli, in which it has been hypothesized that putrescine is first glutamylated to form γ-glutamylputrescine, which is oxidized to 4-(γ-glutamylamino)butanal and then to 4-(γ-glutamylamino)butanoate. The enzyme can also catalyse the reactions of EC 3.5.1.35 (D-glutaminase) and EC 3.5.1.65 (theanine hydrolase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kurihara, S., Oda, S., Kato, K., Kim, H.G., Koyanagi, T., Kumagai, H. and Suzuki, H. A novel putrescine utilization pathway involves γ-glutamylated intermediates of Escherichia coli K-12. J. Biol. Chem. 280 (2005) 4602-4608. [PMID: 15590624]
Accepted name: N-malonylurea hydrolase
Reaction: 3-oxo-3-ureidopropanoate + H2O = malonate + urea
For diagram, click here
Other name(s): ureidomalonase
Systematic name: 3-oxo-3-ureidopropanoate amidohydrolase (urea- and malonate-forming)
Comments: Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 1.17.99.4 (uracil/thymine dehydrogenase) and EC 3.5.2.1 (barbiturase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 368888-22-6
References:
1. Soong, C.L., Ogawa, J. and Shimizu, S. Novel amidohydrolytic reactions in oxidative pyrimidine metabolism: analysis of the barbiturase reaction and discovery of a novel enzyme, ureidomalonase. Biochem. Biophys. Res. Commun. 286 (2001) 222-226. [PMID: 11485332]
2. Soong, C.L., Ogawa, J., Sakuradani, E. and Shimizu, S. Barbiturase, a novel zinc-containing amidohydrolase involved in oxidative pyrimidine metabolism. J. Biol. Chem. 277 (2002) 7051-7058. [PMID: 11748240]
Accepted name: succinylglutamate desuccinylase
Reaction: N-succinyl-L-glutamate + H2O = succinate + L-glutamate
For diagram, click here
Other name(s): N2-succinylglutamate desuccinylase; SGDS; AstE
Systematic name: N-succinyl-L-glutamate amidohydrolase
Comments: Requires Co2+ for maximal activity [1]. N2-Acetylglutamate is not a substrate. This is the final enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine [1]. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.11 (acetylornithine transaminase), EC 1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 99676-40-1
References:
1. Vander Wauven, C. and Stalon, V. Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia. J. Bacteriol. 164 (1985) 882-886. [PMID: 2865249]
2. Cunin, R., Glansdorff, N., Pierard, A. and Stalon, V. Biosynthesis and metabolism of arginine in bacteria. Microbiol. Rev. 50 (1986) 314-352. [PMID: 3534538]
3. Itoh, Y. Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa. J. Bacteriol. 179 (1997) 7280-7290. [PMID: 9393691]
4. Schneider, B.L., Kiupakis, A.K. and Reitzer, L.J. Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli. J. Bacteriol. 180 (1998) 4278-4286. [PMID: 9696779]
Accepted name: acyl-homoserine-lactone acylase
Reaction: an N-acyl-L-homoserine lactone + H2O = L-homoserine lactone + a carboxylate
Other name(s): acyl-homoserine lactone acylase; AHL-acylase; AiiD; N-acyl-homoserine lactone acylase; PA2385 protein; quorum-quenching AHL acylase; quorum-quenching enzyme; PvdQ; QuiP
Systematic name: N-acyl-L-homoserine-lactone amidohydrolase
Comments: Acyl-homoserine lactones (AHLs) are produced by a number of bacterial species and are used by them to regulate the expression of virulence genes in a process known as quorum-sensing. Each bacterial cell has a basal level of AHL and, once the population density reaches a critical level, it triggers AHL-signalling which, in turn, initiates the expression of particular virulence genes. Plants or animals capable of degrading AHLs would have a therapeutic advantage in avoiding bacterial infection as they could prevent AHL-signalling and the expression of virulence genes in quorum-sensing bacteria. This quorum-quenching enzyme removes the fatty-acid side chain from the homoserine lactone ring of AHL-dependent quorum-sensing signal molecules [1]. It has broad specificity for AHLs with side changes ranging in length from 11 to 14 carbons. Substituents at the 3'-position, as found in N-(3-oxododecanoyl)-L-homoserine lactone, do not affect this activity [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Sio, C.F., Otten, L.G., Cool, R.H., Diggle, S.P., Braun, P.G., Bos, R., Daykin, M., Cámara, M., Williams, P. and Quax, W.J. Quorum quenching by an N-acyl-homoserine lactone acylase from Pseudomonas aeruginosa PAO1. Infect. Immun. 74 (2006) 1673-1682. [PMID: 16495538]
2. Lin, Y.H., Xu, J.L., Hu, J., Wang, L.H., Ong, S.L., Leadbetter, J.R. and Zhang, L.H. Acyl-homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum-quenching enzymes. Mol. Microbiol. 47 (2003) 849-860. [PMID: 12535081]
Accepted name: histone deacetylase
Reaction: Hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone
Other name(s): HDAC
Systematic name: histone amidohydrolase
Comments: A class of enzymes that remove acetyl groups from N6-acetyl-lysine residues on a histone. The reaction of this enzyme is opposite to that of EC 2.3.1.48, histone acetyltransferase. Histone deacetylases (HDACs) can be organized into three classes, HDAC1, HDAC2 and HDAC3, depending on sequence similarity and domain organization. Histone acetylation plays an important role in regulation of gene expression. In eukaryotes, HDACs play a key role in the regulation of transcription and cell proliferation [4]. May be identical to EC 3.5.1.17, acyl-lysine deacylase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Krieger, D.E., Levine, R., Merrifield, R.B., Vidali, G. and Allfrey, V.G. Chemical studies of histone acetylation. Substrate specificity of a histone deacetylase from calf thymus nuclei. J. Biol. Chem. 249 (1974) 332-334. [PMID: 4855628]
2. Sanchez del Pino, M.M., Lopez-Rodas, G., Sendra, R. and Tordera, V. Properties of the yeast nuclear histone deacetylase. Biochem. J. 303 (1994) 723-729. [PMID: 7980438]
3. Ouaissi, M. and Ouaissi, A. Histone deacetylase enzymes as potential drug targets in cancer and parasitic diseases. J. Biomed. Biotechnol. 2006 (2006) 13474 only. [PMID: 16883049]
4. Song, Y.M., Kim, Y.S., Kim, D., Lee, D.S. and Kwon, H.J. Cloning, expression, and biochemical characterization of a new histone deacetylase-like protein from Thermus caldophilus GK24. Biochem. Biophys. Res. Commun. 361 (2007) 55-61. [PMID: 17632079]
5. Finnin, M.S., Donigian, J.R., Cohen, A., Richon, V.M., Rifkind, R.A., Marks, P.A., Breslow, R. and Pavletich, N.P. Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature 401 (1999) 188-193. [PMID: 10490031]
6. Phiel, C.J., Zhang, F., Huang, E.Y., Guenther, M.G., Lazar, M.A. and Klein, P.S. Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen. J. Biol. Chem. 276 (2001) 36734-36741. [PMID: 11473107]
7. de Ruijter, A.J., van Gennip, A.H., Caron, H.N., Kemp, S. and van Kuilenburg, A.B. Histone deacetylases (HDACs): characterization of the classical HDAC family. Biochem. J. 370 (2003) 737-749. [PMID: 12429021]
Accepted name: fatty acid amide hydrolase
Reaction: (1) anandamide + H2O = arachidonic acid + ethanolamine
(2) oleamide + H2O = oleic acid + NH3
Glossary: anandamide = (5Z,8Z,11Z,14Z)-N-(2-hydroxyethyl)icosa-5,8,11,14-tetraenamide
Other name(s): FAAH; oleamide hydrolase; anandamide amidohydrolase
Systematic name: fatty acylamide amidohydrolase
Comments: Integral membrane protein, the enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide, occurs in mammalia.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Boger, D.L., Fecik, R.A., Patterson, J.E., Miyauchi, H., Patricelli, M.P. and Cravatt, B.F. Fatty acid amide hydrolase substrate specificity. Bioorg. Med. Chem. Lett. 10 (2000) 2613-2616. [PMID: 11128635]
2. Patricelli, M.P., Lashuel, H.A., Giang, D.K., Kelly, J.W. and Cravatt, B.F. Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: identification of the transmembrane domain as a site for oligomerization. Biochemistry 37 (1998) 15177-15187. [PMID: 9790682]
3. Patricelli, M.P. and Cravatt, B.F. Characterization and manipulation of the acyl chain selectivity of fatty acid amide hydrolase. Biochemistry 40 (2001) 6107-6115. [PMID: 11352748]
Accepted name: (R)-amidase
Reaction: (1) (R)-piperazine-2-carboxamide + H2O = (R)-piperazine-2-carboxylic acid + NH3
(2) β-alaninamide + H2O = β-alanine + NH3
Other name(s): R-stereospecific amidase; R-amidase
Systematic name: (R)-piperazine-2-carboxamide amidohydrolase
Comments: In addition (R)-piperidine-3-carboxamide is hydrolysed to (R)-piperidine-3-carboxylic acid and NH3, and (R)-N-tert-butylpiperazine-2-carboxamide is hydrolysed to (R)-piperazine-2-carboxylic acid and tert-butylamine with lower activity. The enzyme does not act on the other amide substrates which are hydrolysed by EC 3.5.1.4 (amidase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Komeda, H., Harada, H., Washika, S., Sakamoto, T., Ueda, M. and Asano, Y. A novel R-stereoselective amidase from Pseudomonas sp. MCI3434 acting on piperazine-2-tert-butylcarboxamide. Eur. J. Biochem. 271 (2004) 1580-1590. [PMID: 15066183]
Accepted name: L-proline amide hydrolase
Reaction: (1) (S)-piperidine-2-carboxamide + H2O = (S)-piperidine-2-carboxylic acid + NH3
(2) L-prolinamide + H2O = L-proline + NH3
Glossary: L-pipecolate = piperidine-2-carboxylate
Other name(s): S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase; LaaA; L-amino acid amidase
Systematic name: (S)-piperidine-2-carboxamide amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Komeda, H., Harada, H., Washika, S., Sakamoto, T., Ueda, M. and Asano, Y. S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase from Pseudomonas azotoformans IAM 1603 is a novel L-amino acid amidase. Eur. J. Biochem. 271 (2004) 1465-1475. [PMID: 15066172]
Accepted name: 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase
Reaction: 2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + formate
Other name(s): ArfB
Systematic name: 2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one amidohydrolase
Comments: The enzyme catalyses the second step in archaeal riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin biosynthesis. The first step is catalysed by EC 3.5.4.29 (GTP cyclohydrolase IIa). The bacterial enzyme, EC 3.5.4.25 (GTP cyclohydrolase II) catalyses both reactions.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Grochowski, L.L., Xu, H. and White, R.H. An iron(II) dependent formamide hydrolase catalyzes the second step in the archaeal biosynthetic pathway to riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin. Biochemistry 48 (2009) 4181-4188. [PMID: 19309161]
Accepted name: N-acetyl-1D-myo-inositol-2-amino-2-deoxy-α-D-glucopyranoside deacetylase
Reaction: 1-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol + H2O = 1-(2-amino-2-deoxy-α-D-glucopyranoside)-1D-myo-inositol + acetate
For diagram of reaction click here
Glossary: mycothiol = 1-O-[2-(N2-acetyl-L-cysteinamido)-2-deoxy--D-glucopyranosyl]-1D-myo-inositol
Other name(s): MshB
Systematic name: 1-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol acetylhydrolase
Comments: This enzyme is considered the key enzyme and rate limiting step in the mycothiol biosynthesis pathway [1]. In addition to acetylase activity, the enzyme possesses weak mycothiol conjugate amidase activity, and shares sequence similarity with mycothiol S-conjugate amidase [2]. The enzyme requires a divalent transition metal ion for activity, believed to be Zn2+ [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Rawat, M., Kovacevic, S., Billman-Jacobe, H. and Av-Gay, Y. Inactivation of mshB, a key gene in the mycothiol biosynthesis pathway in Mycobacterium smegmatis. Microbiology 149 (2003) 1341-1349. [PMID: 12724395]
2. Newton, G.L., Av-Gay, Y. and Fahey, R.C. N-Acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside deacetylase (MshB) is a key enzyme in mycothiol biosynthesis. J. Bacteriol. 182 (2000) 6958-6963. [PMID: 11092856]
3. Maynes, J.T., Garen, C., Cherney, M.M., Newton, G., Arad, D., Av-Gay, Y., Fahey, R.C. and James, M.N. The crystal structure of 1-D-myo-inosityl 2-acetamido-2-deoxy-α-D-glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis reveals a zinc hydrolase with a lactate dehydrogenase fold. J. Biol. Chem. 278 (2003) 47166-47170. [PMID: 12958317]
Accepted name: peptidoglycan-N-acetylglucosamine deacetylase
Reaction: peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-glucosamine + acetate
Other name(s): HP310; PgdA; SpPgdA; BC1960; peptidoglycan deacetylase; N-acetylglucosamine deacetylase; peptidoglycan GlcNAc deacetylase; peptidoglycan N-acetylglucosamine deacetylase; PG N-deacetylase
Systematic name: peptidoglycan-N-acetylglucosamine amidohydrolase
Comments: Modification of peptidoglycan by N-deacetylation is an important factor in virulence of Helicobacter pylori, Listeria monocytogenes and Streptococcus suis [4-6]. The enzyme from Streptococcus pneumoniae is a metalloenzyme using a His-His-Asp zinc-binding triad with a nearby aspartic acid and histidine acting as the catalytic base and acid, respectively [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Psylinakis, E., Boneca, I.G., Mavromatis, K., Deli, A., Hayhurst, E., Foster, S.J., Varum, K.M. and Bouriotis, V. Peptidoglycan N-acetylglucosamine deacetylases from Bacillus cereus, highly conserved proteins in Bacillus anthracis. J. Biol. Chem. 280 (2005) 30856-30863. [PMID: 15961396]
2. Tsalafouta, A., Psylinakis, E., Kapetaniou, E.G., Kotsifaki, D., Deli, A., Roidis, A., Bouriotis, V. and Kokkinidis, M. Purification, crystallization and preliminary X-ray analysis of the peptidoglycan N-acetylglucosamine deacetylase BC1960 from Bacillus cereus in the presence of its substrate (GlcNAc)6. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 (2008) 203-205. [PMID: 18323609]
3. Blair, D.E., Schuttelkopf, A.W., MacRae, J.I. and van Aalten, D.M. Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor. Proc. Natl. Acad. Sci. USA 102 (2005) 15429-15434. [PMID: 16221761]
4. Wang, G., Olczak, A., Forsberg, L.S. and Maier, R.J. Oxidative stress-induced peptidoglycan deacetylase in Helicobacter pylori. J. Biol. Chem. 284 (2009) 6790-6800. [PMID: 19147492]
5. Popowska, M., Kusio, M., Szymanska, P. and Markiewicz, Z. Inactivation of the wall-associated de-N-acetylase (PgdA) of Listeria monocytogenes results in greater susceptibility of the cells to induced autolysis. J Microbiol Biotechnol 19 (2009) 932-945. [PMID: 19809250]
6. Fittipaldi, N., Sekizaki, T., Takamatsu, D., de la Cruz Domínguez-Punaro, M., Harel, J., Bui, N.K., Vollmer, W. and Gottschalk, M. Significant contribution of the pgdA gene to the virulence of Streptococcus suis. Mol. Microbiol. 70 (2008) 1120-1135. [PMID: 18990186]
Accepted name: chitin disaccharide deacetylase
Reaction: 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-β-D-glucopyranosyl]-2-deoxy-β-D-glucopyranose + H2O = 2-(acetylamino)-4-O-(2-amino-2-deoxy-β-D-glucopyranosyl)-2-deoxy-β-D-glucopyranose + acetate
Other name(s): chitobiose amidohydolase; COD; chitin oligosaccharide deacetylase; chitin oligosaccharide amidohydolase
Systematic name: 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-β-D-glucopyranosyl]-2-deoxy-D-glucopyranose acetylhydrolase
Comments: Chitin oligosaccharide deacetylase is a key enzyme in the chitin catabolic cascade of chitinolytic Vibrio strains. Besides being a nutrient, the heterodisaccharide product 4-O-(N-acetyl-β-D-glucosaminyl)-D-glucosamine is a unique inducer of chitinase production in Vibrio parahaemolyticus [2]. In contrast to EC 3.5.1.41 (chitin deacetylase) this enzyme is specific for the chitin disaccharide [1,3]. It also deacetylates the chitin trisaccharide with lower efficiency [3]. No activity with higher polymers of GlcNAc [1,3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kadokura, K., Rokutani, A., Yamamoto, M., Ikegami, T., Sugita, H., Itoi, S., Hakamata, W., Oku, T. and Nishio, T. Purification and characterization of Vibrio parahaemolyticus extracellular chitinase and chitin oligosaccharide deacetylase involved in the production of heterodisaccharide from chitin. Appl. Microbiol. Biotechnol. 75 (2007) 357-365. [PMID: 17334758]
2. Hirano, T., Kadokura, K., Ikegami, T., Shigeta, Y., Kumaki, Y., Hakamata, W., Oku, T. and Nishio, T. Heterodisaccharide 4-O-(N-acetyl-β-D-glucosaminyl)-D-glucosamine is a specific inducer of chitinolytic enzyme production in Vibrios harboring chitin oligosaccharide deacetylase genes. Glycobiology 19 (2009) 1046-1053. [PMID: 19553519]
3. Ohishi, K., Yamagishi, M., Ohta, T., Motosugi, M., Izumida, H., Sano, H., Adachi, K., Miwa, T. Purification and properties of two deacetylases produced by Vibrio alginolyticus H-8. Biosci. Biotechnol. Biochem. 61 (1997) 1113-1117.
4. Ohishi, K., Murase, K., Ohta, T. and Etoh, H. Cloning and sequencing of the deacetylase gene from Vibrio alginolyticus H-8. J. Biosci. Bioeng. 90 (2000) 561-563. [PMID: 16232910]
Accepted name: N-formylmaleamate deformylase
Reaction: N-formylmaleamic acid + H2O = maleamate + formate
Other name(s): NicD
Systematic name: N-formylmaleamic acid amidohydrolase
Comments: The reaction is involved in the aerobic catabolism of nicotinic acid.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Jimenez, J.I., Canales, A., Jimenez-Barbero, J., Ginalski, K., Rychlewski, L., Garcia, J.L. and Diaz, E. Deciphering the genetic determinants for aerobic nicotinic acid degradation: the nic cluster from Pseudomonas putida KT2440. Proc. Natl. Acad. Sci. USA 105 (2008) 11329-11334. [PMID: 18678916]
Accepted name: maleamate amidohydrolase
Reaction: maleamate + H2O = maleate + NH3
Other name(s): NicF
Systematic name: maleamate amidohydrolase
Comments: The reaction is involved in the aerobic catabolism of nicotinic acid.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Jimenez, J.I., Canales, A., Jimenez-Barbero, J., Ginalski, K., Rychlewski, L., Garcia, J.L. and Diaz, E. Deciphering the genetic determinants for aerobic nicotinic acid degradation: the nic cluster from Pseudomonas putida KT2440. Proc. Natl. Acad. Sci. USA 105 (2008) 11329-11334. [PMID: 18678916]
Accepted name: UDP-3-O-acyl-N-acetylglucosamine deacetylase
Reaction: UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-α-D-glucosamine + H2O = UDP-3-O-[(3R)-3-hydroxymyristoyl]-α-D-glucosamine + acetate
Other name(s): LpxC protein; LpxC enzyme; LpxC deacetylase; deacetylase LpxC; UDP-3-O-acyl-GlcNAc deacetylase; UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase; UDP-(3-O-acyl)-N-acetylglucosamine deacetylase; UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase; UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase; UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetylglucosamine amidohydrolase
Systematic name: UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetylglucosamine amidohydrolase
Comments: A zinc protein. The enzyme catalyses a committed step in the biosynthesis of lipid A.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hernick, M., Gennadios, H.A., Whittington, D.A., Rusche, K.M., Christianson, D.W. and Fierke, C.A. UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism. J. Biol. Chem. 280 (2005) 16969-16978. [PMID: 15705580]
2. Jackman, J.E., Raetz, C.R. and Fierke, C.A. UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme. Biochemistry 38 (1999) 1902-1911. [PMID: 10026271]
3. Hyland, S.A., Eveland, S.S. and Anderson, M.S. Cloning, expression, and purification of UDP-3-O-acyl-GlcNAc deacetylase from Pseudomonas aeruginosa: a metalloamidase of the lipid A biosynthesis pathway. J. Bacteriol. 179 (1997) 2029-2037. [PMID: 9068651]
4. Wang, W., Maniar, M., Jain, R., Jacobs, J., Trias, J. and Yuan, Z. A fluorescence-based homogeneous assay for measuring activity of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase. Anal. Biochem. 290 (2001) 338-346. [PMID: 11237337]
5. Whittington, D.A., Rusche, K.M., Shin, H., Fierke, C.A. and Christianson, D.W. Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis. Proc. Natl. Acad. Sci. USA 100 (2003) 8146-8150. [PMID: 12819349]
6. Mochalkin, I., Knafels, J.D. and Lightle, S. Crystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitor. Protein Sci. 17 (2008) 450-457. [PMID: 18287278]
Accepted name: sphingomyelin deacylase
Reaction: (1) an N-acyl-sphingosylphosphorylcholine + H2O = a fatty acid + sphingosylphosphorylcholine
(2) a D-glucosyl-N-acylsphingosine + H2O = a fatty acid + D-glucosyl-sphingosine
Glossary: sphingomyelin = N-acyl-sphingosylphosphorylcholine
D-glucosyl-N-acylsphingosine = glucosylceramide
Other name(s): SM deacylase; GcSM deacylase; glucosylceramide sphingomyelin deacylase; sphingomyelin glucosylceramide deacylase; SM glucosylceramide GCer deacylase; SM-GCer deacylase; SMGCer deacylase
Systematic name: N-acyl-sphingosylphosphorylcholine amidohydrolase
Comments: The enzyme is involved in the sphingolipid metabolism in the epidermis.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hara, J., Higuchi, K., Okamoto, R., Kawashima, M. and Imokawa, G. High-expression of sphingomyelin deacylase is an important determinant of ceramide deficiency leading to barrier disruption in atopic dermatitis. J. Invest. Dermatol. 115 (2000) 406-413. [PMID: 10951276]
2. Higuchi, K., Hara, J., Okamoto, R., Kawashima, M. and Imokawa, G. The skin of atopic dermatitis patients contains a novel enzyme, glucosylceramide sphingomyelin deacylase, which cleaves the N-acyl linkage of sphingomyelin and glucosylceramide. Biochem. J. 350 (2000) 747-756. [PMID: 10970788]
3. Ishibashi, M., Arikawa, J., Okamoto, R., Kawashima, M., Takagi, Y., Ohguchi, K. and Imokawa, G. Abnormal expression of the novel epidermal enzyme, glucosylceramide deacylase, and the accumulation of its enzymatic reaction product, glucosylsphingosine, in the skin of patients with atopic dermatitis. Lab. Invest. 83 (2003) 397-408. [PMID: 12649340]
Accepted name: peroxyureidoacrylate/ureidoacrylate amidohydrolase
Reaction: (1) (Z)-3-ureidoacrylate peracid + H2O = (Z)-3-peroxyaminoacrylate + CO2 + NH3 (overall reaction)
(1a) (Z)-3-ureidoacrylate peracid + H2O = (Z)-3-peroxyaminoacrylate + carbamate
(1b) carbamate = CO2 + NH3 (spontaneous)
(2) (Z)-2-methylureidoacrylate peracid + H2O = (Z)-2-methylperoxyaminoacrylate + CO2 + NH3 (overall reaction)
(2a) (Z)-2-methylureidoacrylate peracid + H2O = (Z)-2-methylperoxyaminoacrylate + carbamate
(2b) carbamate = CO2 + NH3 (spontaneous)
Glossary: ureidoperacrylic acid = (Z)-3-ureidoacrylate peracid = (2Z)-3-(carbamoylamino)prop-2-eneperoxoic acid
(Z)-2-methylureidoperacrylic acid = (Z)-2-methylureidoacrylate peracid = (2Z)-3-(carbamoylamino)-2-methylprop-2-eneperoxoic acid
Other name(s): RutB
Systematic name: (Z)-3-ureidoacrylate peracid amidohydrolase
Comments: The enzyme also shows activity towards ureidoacrylate. Part of the Rut pyrimidine catabolic pathway.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kim, K.S., Pelton, J.G., Inwood, W.B., Andersen, U., Kustu, S. and Wemmer, D.E. The Rut pathway for pyrimidine degradation: novel chemistry and toxicity problems. J. Bacteriol. 192 (2010) 4089-4102. [PMID: 20400551]
Accepted name: 2-oxoglutaramate amidase
Reaction: 2-oxoglutaramate + H2O = 2-oxoglutarate + ammonia
Glossary: 2-oxoglutaramate = 2-ketoglutaramate = 5-amino-2,5-dioxopentanoate
Other name(s): ω-amidase (ambiguous)
Systematic name: 5-amino-2,5-dioxopentanoate amidohydrolase
Comments: The enzyme, which is highly specific for its substrate, participates in the nicotine degradation pathway of several Gram-positive bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Cobzaru, C., Ganas, P., Mihasan, M., Schleberger, P. and Brandsch, R. Homologous gene clusters of nicotine catabolism, including a new ω-amidase for α-ketoglutaramate, in species of three genera of Gram-positive bacteria. Res. Microbiol. 162 (2011) 285-291. [PMID: 21288482]
Accepted name: 2'-N-acetylparomamine deacetylase
Reaction: 2'-N-acetylparomamine + H2O = paromamine + acetate
For diagram of reaction click here.
Glossary: paromamine = (1R)-O4-(2-amino-2-deoxy-α-D-glucopyranosyl)-2-deoxy-streptamine
Other name(s): btrD (gene name); neoL (gene name); kanN (gene name)
Systematic name: 2'-N-acetylparomamine hydrolase (acetate-forming)
Comments: Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. The enzyme from the bacterium Streptomyces fradiae can also accept 2'''-acetyl-6'''-hydroxyneomycin C as substrate, cf. EC 3.5.1.113, 2'''-acetyl-6'''-hydroxyneomycin C deacetylase [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Truman, A.W., Huang, F., Llewellyn, N.M. and Spencer, J.B. Characterization of the enzyme BtrD from Bacillus circulans and revision of its functional assignment in the biosynthesis of butirosin. Angew. Chem. Int. Ed. Engl. 46 (2007) 1462-1464. [PMID: 17226887]
2. Yokoyama, K., Yamamoto, Y., Kudo, F. and Eguchi, T. Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis. ChemBioChem. 9 (2008) 865-869. [PMID: 18311744]
Accepted name: 2'''-acetyl-6'''-hydroxyneomycin C deacetylase
Reaction: 2'''-acetyl-6'''-deamino-6'''-hydroxyneomycin C + H2O = 6'''-deamino-6'''-hydroxyneomycin C + acetate
For diagram of reaction click here.
Other name(s): neoL (gene name)
Systematic name: 2'''-acetyl-6'''-hydroxyneomycin C hydrolase (acetate-forming)
Comments: Involved in the biosynthetic pathway of aminoglycoside antibiotics of the neomycin family. The enzyme from the bacterium Streptomyces fradiae also catalyses EC 3.5.1.112, 2'-N-acetylparomamine deacetylase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yokoyama, K., Yamamoto, Y., Kudo, F. and Eguchi, T. Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis. ChemBioChem. 9 (2008) 865-869. [PMID: 18311744]