Continued from EC 3.2.1.151 to 3.2.1.184
EC 3.2.2 Hydrolysing N-Glycosyl Compounds
EC 3.2.3 Hydrolysing S-Glycosyl Compounds
Accepted name: purine nucleosidase
Reaction: a purine nucleoside + H2O = D-ribose + a purine base
Other name(s): nucleosidase (misleading); purine β-ribosidase; purine nucleoside hydrolase; purine ribonucleosidase; ribonucleoside hydrolase (misleading); nucleoside hydrolase (misleading); N-ribosyl purine ribohydrolase; nucleosidase g; N-D-ribosylpurine ribohydrolase; inosine-adenosine-guanosine preferring nucleoside hydrolase; purine-specific nucleoside N-ribohydrolase; IAG-nucleoside hydrolase; IAG-NH
Systematic name: purine-nucleoside ribohydrolase
Comments: The enzyme from the bacterium Ochrobactrum anthropi specifically catalyses the irreversible N-riboside hydrolysis of purine nucleosides. Pyrimidine nucleosides, purine and pyrimidine nucleotides, NAD+, NADP+ and nicotinaminde mononucleotide are not substrates [6].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-44-9
References:
1. Heppel, L.A. and Hilmoe, R.J. Phosphorolysis and hydrolysis of purine ribosides from yeast. J. Biol. Chem. 198 (1952) 683-694. [PMID: 12999785]
2. Kalckar, H.M. Biosynthetic aspects of nucleosides and nucleic acids. Pubbl. Staz. Zool. (Napoli) 23 (1951) 87-103.
3. Takagi, Y. and Horecker, B.L. Purification and properties of a bacterial riboside hydrolyase. J. Biol. Chem. 225 (1956) 77-86. [PMID: 13416219]
4. Tarr, H.L.A. Fish muscle riboside hydrolases. Biochem. J. 59 (1955) 386-391. [PMID: 14363106]
5. Parkin, D.W. Purine-specific nucleoside N-ribohydrolase from Trypanosoma brucei brucei. Purification, specificity, and kinetic mechanism. J. Biol. Chem. 271 (1996) 21713-21719. [PMID: 8702965]
6. Ogawa, J., Takeda, S., Xie, S.X., Hatanaka, H., Ashikari, T., Amachi, T. and Shimizu, S. Purification, characterization, and gene cloning of purine nucleosidase from Ochrobactrum anthropi. Appl. Environ. Microbiol. 67 (2001) 1783-1787. [PMID: 11282633]
7. Versées, W., Decanniere, K., Van Holsbeke, E., Devroede, N. and Steyaert, J. Enzyme-substrate interactions in the purine-specific nucleoside hydrolase from Trypanosoma vivax. J. Biol. Chem. 277 (2002) 15938-15946. [PMID: 11854281]
8. Mazumder-Shivakumar, D. and Bruice, T.C. Computational study of IAG-nucleoside hydrolase: determination of the preferred ground state conformation and the role of active site residues. Biochemistry 44 (2005) 7805-7817. [PMID: 15909995]
Accepted name: inosine nucleosidase
Reaction: inosine + H2O = D-ribose + hypoxanthine
Other name(s): inosinase; inosine-guanosine nucleosidase
Systematic name: inosine ribohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9030-95-9
References:
1. Koch, A.L. Some enzymes of nucleoside metabolism of Escherichia coli. J. Biol. Chem. 223 (1956) 535-549.
2. Tarr, H.L.A. Fish muscle riboside hydrolases. Biochem. J. 59 (1955) 386-391.
Accepted name: uridine nucleosidase
Reaction: uridine + H2O = D-ribose + uracil
Other name(s): uridine hydrolase
Systematic name: uridine ribohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-47-2
References:
1. Carter, C.E. Partial purification of a non-phosphorylytic uridine nucleosidase from yeast. J. Am. Chem. Soc. 73 (1951) 1508-1510.
Accepted name: AMP nucleosidase
Reaction: AMP + H2O = D-ribose 5-phosphate + adenine
Other name(s): adenylate nucleosidase; adenosine monophosphate nucleosidase
Systematic name: AMP phosphoribohydrolase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9025-45-0
References:
1. Hurwitz, J., Heppel, L.A. and Horecker, B.L. The enzymatic cleavage of adenylic acid to adenine and ribose 5-phosphate. J. Biol. Chem. 226 (1957) 525-540.
Accepted name: NAD+ nucleosidase
Reaction: NAD+ + H2O = ADP-ribose + nicotinamide
Other name(s): NADase; DPNase; DPN hydrolase; NAD hydrolase; diphosphopyridine nucleosidase; nicotinamide adenine dinucleotide nucleosidase; NAD glycohydrolase; NAD nucleosidase; nicotinamide adenine dinucleotide glycohydrolase
Systematic name: NAD+ glycohydrolase
Comments: This enzyme can also hydrolyse NADP+ to yield phospho-ADP-ribose and nicotinamide, but more slowly.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9032-65-9
References:
1. Hofmann, E.C.G. and Rapoport, S. DPN- und TPN-spezifische Nukleosidasen in Erythrozyten. Biochim. Biophys. Acta 18 (1955) 296 only.
2. Nakazawa, K., Ueda, K., Honjo, T., Yoshihara, K., Nishizuka, Y. and Hayaishi, O. Nicotinamide adenine dinucleotide glycohydrolases and poly adenosine diphosphate ribose synthesis in rat liver. Biochem. Biophys. Res. Commun. 32 (1968) 143-149. [PMID: 5672131]
3. Ueda, K., Fukushima, M., Okayamo, H. and Hayaishi, O. Nicotinamide adenine dinucleotide glycohydrolase from rat liver nuclei. Isolation and characterization of a new enzyme. J. Biol. Chem. 250 (1975) 7541-7546. [PMID: 240831]
4. Yamamoto-Katayama, S., Ariyoshi, M., Ishihara, K., Hirano, T., Jingami, H. and Morikawa, K. Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities. J. Mol. Biol. 316 (2002) 711-723. [PMID: 11866528]
Accepted name: NAD-glycohydrolase
Reaction: NAD+ + H2O = ADP-D-ribose + nicotinamide
Glossary: ADP-D-ribose = adenosine 5'-(5-deoxy-D-ribofuranos-5-yl diphosphate)
Other name(s): NADase; nga (gene name)
Systematic name: NAD+ glycohydrolase
Comments: The enzyme catalyses the hydrolysis of NAD+, without associated ADP-ribosyl transferase or ADP-ribosyl cyclase activities. The enzyme from Group A streptococci has been implicated in the pathogenesis of diseases such as streptococcal toxic shock-like syndrome (STSS) and necrotizing fasciitis. The enzyme from the venom of the snake Agkistrodon acutus also catalyses EC 3.6.1.5, apyrase [3].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9025-46-1
References:
1. Alivasatos, S.G.A. and Woolley, D.W. Solubilization and purification of the diphosphopyridine nucleotidase from beef spleen. J. Biol. Chem. 219 (1956) 823-832.
2. Zatman, L.J., Kaplan, N.O. and Colowick, S.P. Inhibition of spleen diphosphopyridine nucleotidase by nicotinamide, an exchange reaction. J. Biol. Chem. 200 (1953) 197-212.
3. Zatman, L.J., Kaplan, N.O., Colowick, S.P. and Ciotti, M.M. Formation of the isonicotinic acid hydrazide analog of DPN. J. Am. Chem. Soc. 75 (1953) 3293-3294.
Accepted name: adenosine nucleosidase
Reaction: adenosine + H2O = D-ribose + adenine
Other name(s): adenosinase; N-ribosyladenine ribohydrolase; adenosine hydrolase; ANase
Systematic name: adenosine ribohydrolase
Comments: Also acts on adenosine N-oxide.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9075-41-6
References:
1. Mazelis, M. and Creveling, R.K. An adenosine hydrolase from brussels sprouts. J. Biol. Chem. 238 (1963) 3358-3361.
Accepted name: ribosylpyrimidine nucleosidase
Reaction: a pyrimidine nucleoside + H2O = D-ribose + a pyrimidine base
Other name(s): N-ribosylpyrimidine nucleosidase; pyrimidine nucleosidase; N-ribosylpyrimidine ribohydrolase; pyrimidine nucleoside hydrolase; RihB; YeiK; nucleoside ribohydrolase
Systematic name: pyrimidine-nucleoside ribohydrolase
Comments: Also hydrolyses purine D-ribonucleosides, but more slowly. 2'-, 3'- and 5'-deoxynucleosides are not substrates [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37288-60-1
References:
1. Terada, M., Tatibana, M. and Hayaishi, O. Preparation and properties of nucleoside hydrolase from Pseudomonas fluorescens. J. Biol. Chem. 242 (1967) 5578-5585. [PMID: 12325375]
2. Petersen, C. and Møller, L.B. The RihA, RihB, and RihC ribonucleoside hydrolases of Escherichia coli. Substrate specificity, gene expression, and regulation. J. Biol. Chem. 276 (2001) 884-894. [PMID: 11027694]
3. Giabbai, B. and Degano, M. Cloning, purification, crystallization and X-ray analysis of the Escherichia coli pyrimidine nucleoside hydrolase YeiK. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 524-527. [PMID: 14993681]
4. Giabbai, B. and Degano, M. Crystal structure to 1.7 Å of the Escherichia coli pyrimidine nucleoside hydrolase YeiK, a novel candidate for cancer gene therapy. Structure 12 (2004) 739-749. [PMID: 15130467]
Accepted name: adenosylhomocysteine nucleosidase
Reaction: S-adenosyl-L-homocysteine + H2O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine
For diagram click here or here.
Other name(s): S-adenosylhomocysteine hydrolase (ambiguous); S-adenosylhomocysteine nucleosidase; 5'-methyladenosine nucleosidase; S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase; AdoHcy/MTA nucleosidase
Systematic name: S-adenosyl-L-homocysteine homocysteinylribohydrolase
Comments: Also acts on S-methyl-5'-thioadenosine to give adenine and S-methyl-5-thioribose (cf. EC 3.2.2.16, methylthioadenosine nucleosidase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9055-10-1
References:
1. Duerre, J.A. A hydrolytic nucleosidase acting on S-adenosylhomocysteine and on 5-methylthioadenosine. J. Biol. Chem. 237 (1962) 3737-3741.
2. Ferro, A.J., Barrett, A. and Shapiro, S.K. Kinetic properties and the effect of substrate analogues on 5'-methylthioadenosine nucleosidase from Escherichia coli. Biochim. Biophys. Acta 438 (1976) 487-494. [PMID: 782530]
Accepted name: pyrimidine-5'-nucleotide nucleosidase
Reaction: a pyrimidine 5'-nucleotide + H2O = D-ribose 5-phosphate + a pyrimidine base
Other name(s): pyrimidine nucleotide N-ribosidase; Pyr5N
Systematic name: pyrimidine-5'-nucleotide phosphoribo(deoxyribo)hydrolase
Comments: Also acts on dUMP, dTMP and dCMP.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9023-31-8
References:
1. Imada, A. Degradation of pyrimidine nucleotides by enzyme systems of Streptomyces. II. Pyrimidine 5'-nucleotide phosphoribo(deoxyribo) hydrolase of Streptomyces virginiae. J. Gen. Appl. Microbiol. 13 (1967) 267-278.
2. Imada, A., Kuno, M. and Igarasi, S. Degradation of pyrimidine nucleotides by enzyme systems of Streptomyces. I. Ribose-5-phosphate formation from pyrimidine nucleotides. J. Gen. Appl. Microbiol. 13 (1967) 255-265.
Accepted name: β-aspartyl-N-acetylglucosaminidase
Reaction: 1-β-aspartyl-N-acetyl-D-glucosaminylamine + H2O = L-asparagine + N-acetyl-D-glucosamine
Other name(s): β-aspartylacetylglucosaminidase
Systematic name: 1-β-aspartyl-N-acetyl-D-glucosaminylamine L-asparaginohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9027-31-0
References:
1. Eylar, E.H. and Murakami, M. β-Aspartyl-N-acetylglucosaminidase from epididymis. Methods Enzymol. 8 (1966) 597-600.
Accepted name: inosinate nucleosidase
Reaction: IMP + H2O = D-ribose 5-phosphate + hypoxanthine
For diagram click here.
Glossary: IMP = inosine 5'-phosphate
Other name(s): 5'-inosinate phosphoribohydrolase
Systematic name: IMP phosphoribohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37288-61-2
References:
1. Kuninaka, A. 5'-Inosinic acid-N-ribosidase in Aspergillus. Koso Kagaka Shinojiumu 12 (1957) 65-69.
Accepted name: 1-methyladenosine nucleosidase
Reaction: 1-methyladenosine + H2O = 1-methyladenine + D-ribose
Other name(s): 1-methyladenosine hydrolase
Systematic name: 1-methyladenosine ribohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37367-71-8
References:
1. Tarr, H.L.A. 1-Methyladenosine hydrolase of starfish (Pisaster ochraceous). J. Fish Res. Board Can. 30 (1973) 1861-1866.
Accepted name: NMN nucleosidase
Reaction: nicotinamide β-D-ribonucleotide + H2O = D-ribose 5-phosphate + nicotinamide
Other name(s): NMNase; nicotinamide mononucleotide nucleosidase; nicotinamide mononucleotidase; NMN glycohydrolase; NMNGhase
Systematic name: nicotinamide-nucleotide phosphoribohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37237-49-3
References:
1. Andreoli, A.J., Okita, T.W., Bloom, R. and Grover, T.A. The pyridine nucleotide cycle: presence of a nicotinamide mononucleotide-specific glycohydrolase in Escherichia coli. Biochem. Biophys. Res. Commun. 49 (1972) 264-269. [PMID: 4342726]
Accepted name: DNA-deoxyinosine glycosylase
Reaction: Hydrolyses DNA and polynucleotides, releasing free hypoxanthine
Other name(s): DNA(hypoxanthine) glycohydrolase; deoxyribonucleic acid glycosylase; hypoxanthine-DNA glycosylase
Systematic name: DNA-deoxyinosine deoxyribohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 68247-62-1
References:
1. Karran, P. and Lindahl, T. Enzymatic excision of free hypoxanthine from polydeoxynucleotides and DNA containing deoxyinosine monophosphate residues. J. Biol. Chem. 253 (1978) 5877-5879. [PMID: 98523]
Accepted name: methylthioadenosine nucleosidase
Reaction: S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine
For diagram click here.
Other name(s): 5'-methylthioadenosine nucleosidase; MTA nucleosidase; MeSAdo nucleosidase; methylthioadenosine methylthioribohydrolase
Systematic name: S-methyl-5'-thioadenosine adeninehyrolase
Comments: Does not act on S-adenosylhomocysteine. cf. EC 3.2.2.9 adenosylhomocysteine nucleosidase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 50812-28-7
References:
1. Guranowski, A.B., Chiang, P.K. and Cantoni, G.L. 5'-Methylthioadenosine nucleosidase. Purification and characterization of the enzyme from Lupinus luteus seeds. Eur. J. Biochem. 114 (1981) 293-299. [PMID: 6783408]
Accepted name: deoxyribodipyrimidine endonucleosidase
Reaction: Cleaves the N-glycosidic bond between the 5'-pyrimidine residue in cyclobutadipyrimidine (in DNA) and the corresponding deoxy-D-ribose residue
Other name(s): pyrimidine dimer DNA-glycosylase; endonuclease V; deoxyribonucleate pyrimidine dimer glycosidase; pyrimidine dimer DNA glycosylase; T4-induced UV endonuclease; PD-DNA glycosylase
Systematic name: deoxy-D-ribocyclobutadipyrimidine polynucleotidodeoxyribohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 75302-33-9
References:
1. Haseltine, W.A., Gordon, L.K., Lindan, C.P., Grafstrom, R.H., Shaper, N.L. and Grossman, L. Cleavage of pyrimidine dimers in specific DNA sequences by a pyrimidine dimer DNA-glycosylase of M. luteus. Nature 285 (1980) 634-641. [PMID: 6248789]
[EC 3.2.2.18 Deleted entry: glycopeptide N-glycosidase. Now included with EC 3.5.1.52 N4-(β-N-acetylglucosaminyl)-L-asparaginase (EC 3.2.2.18 created 1984, deleted 1989)]
Accepted name: [protein ADP-ribosylarginine] hydrolase
Reaction: (1) protein-Nω-(ADP-D-ribosyl)-L-arginine + H2O = ADP-D-ribose + protein-L-arginine
(2) Nω-(ADP-D-ribosyl)-L-arginine + H2O = ADP-ribose + L-arginine
Other name(s): ADP-ribose-L-arginine cleavage enzyme; ADP-ribosylarginine hydrolase; Nω-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase
Systematic name: protein-Nω-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase
Comments: The enzyme will remove ADP-D-ribose from arginine residues in ADP-ribosylated proteins.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 98668-52-1
References:
1. Moss, J., Jacobson, M.K. and Stanley, S.J. Reversibility of arginine-specific mono(ADP-ribosyl)ation: identification in erythrocytes of an ADP-ribose-L-arginine cleavage enzyme. Proc. Natl. Acad. Sci. USA 82 (1985) 5603-5607. [PMID: 2994036]
2. Moss, J., Stanley, S.J., Nightingale, M.S., Murtagh, J.J., Jr., Monaco, L., Mishima, K., Chen, H.C., Williamson, K.C. and Tsai, S.C. Molecular and immunological characterization of ADP-ribosylarginine hydrolases. J. Biol. Chem. 267 (1992) 10481-10488. [PMID: 1375222]
3. Konczalik, P. and Moss, J. Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases. J. Biol. Chem. 274 (1999) 16736-16740. [PMID: 10358013]
4. Takada, T., Iida, K. and Moss, J. Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase. J. Biol. Chem. 268 (1993) 17837-17843 [PMID: 8349667]
5. Ohno, T., Tsuchiya, M., Osago, H., Hara, N., Jidoi, J. and Shimoyama, M. Detection of arginine-ADP-ribosylated protein using recombinant ADP-ribosylarginine hydrolase. Anal. Biochem. 10 (1995) 115-122 [PMID: 8678289]
Accepted name: DNA-3-methyladenine glycosylase I
Reaction: Hydrolysis of alkylated DNA, releasing 3-methyladenine
Other name(s): deoxyribonucleate 3-methyladenine glycosidase I; 3-methyladenine DNA glycosylase I; DNA-3-methyladenine glycosidase I
Systematic name: alkylated-DNA glycohydrolase (releasing methyladenine and methylguanine)
Comments: Involved in the removal of alkylated bases from DNA in Escherichia coli (cf. EC 2.1.1.63 methylated-DNA—[protein]-cysteine S-methyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 89287-37-6
References:
1. Evensen, G. and Seeberg, E. Adaptation to alkylation resistance involves the induction of a DNA glycosylase. Nature 296 (1982) 773-775. [PMID: 7040984]
2. Karran, P., Hjelmgren, T. and Lindahl, T. Induction of a DNA glycosylase for N-methylated purines is part of the adaptive response to alkylating agents. Nature 296 (1982) 770-773. [PMID: 7040983]
3. Thomas, L., Yang, C.-H. and Goldthwait, D.A. Two DNA glycosylases in Escherichia coli which release primarily 3-methyladenine. Biochemistry 21 (1982) 1162-1169. [PMID: 7041972]
Accepted name: DNA-3-methyladenine glycosylase II
Reaction: Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine
Other name(s): deoxyribonucleate 3-methyladenine glycosidase II; 3-methyladenine DNA glycosylase II; DNA-3-methyladenine glycosidase II; AlkA
Systematic name: alkylated-DNA glycohydrolase (releasing methyladenine and methylguanine)
Comments: Involved in the removal of alkylated bases from DNA in Escherichia coli (cf. EC 2.1.1.63 methylated-DNA—[protein]-cysteine S-methyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 89287-38-7
References:
1. Evensen, G. and Seeberg, E. Adaptation to alkylation resistance involves the induction of a DNA glycosylase. Nature 296 (1982) 773-775. [PMID: 7040984]
2. Karran, P., Hjelmgren, T. and Lindahl, T. Induction of a DNA glycosylase for N-methylated purines is part of the adaptive response to alkylating agents. Nature 296 (1982) 770-773. [PMID: 7040983]
3. Riazuddin, S. and Lindahl, T. Properties of 3-methyladenine-DNA glycosylase from Escherichia coli. Biochemistry 17 (1978) 2110-2118. [PMID: 352392]
4. Thomas, L., Yang, C.-H. and Goldthwait, D.A. Two DNA glycosylases in Escherichia coli which release primarily 3-methyladenine. Biochemistry 21 (1982) 1162-1169. [PMID: 7041972]
Accepted name: rRNA N-glycosylase
Reaction: Hydrolysis of the N-glycosylic bond at A-4324 in 28S rRNA from rat ribosomes
Other name(s): ribosomal ribonucleate N-glycosidase; nigrin b; RNA N-glycosidase; rRNA N-glycosidase; ricin; momorcochin-S; Mirabilis antiviral protein; momorcochin-S; gelonin; saporins
Systematic name: rRNA N-glycohydrolase
Comments: Ricin A-chain and related toxins show this activity. Naked rRNA is attacked more slowly than rRNA in intact ribosomes. Naked rRNA from Escherichia coli is cleaved at a corresponding position.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 113756-12-0
References:
1. Endo, Y. and Tsurugi, K. The RNA N-glycosidase activity of ricin A-chain. The characteristics of the enzymatic activity of ricin A-chain with ribosomes and with rRNA. J. Biol. Chem. 263 (1988) 8735-8739. [PMID: 3288622]
Accepted name: DNA-formamidopyrimidine glycosylase
Reaction: Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
Other name(s): Fapy-DNA glycosylase; deoxyribonucleate glycosidase; 2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase; 2,6-diamino-4-hydroxy-5(N-methyl)formamidopyrimidine-DNA glycosylase; formamidopyrimidine-DNA glycosylase; DNA-formamidopyrimidine glycosidase; Fpg protein
Systematic name: DNA glycohydrolase [2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimide releasing]
Comments: May play a significant role in processes leading to recovery from mutagenesis and/or cell death by alkylating agents. Also involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 78783-53-6
References:
1. Boiteux, S., O'Connor, T.R. and Laval J. Formamidopyrimidine-DNA glycosylase of Escherichia coli: cloning and sequencing of the fpg structural gene and overproduction of the protein. EMBO J. 6 (1987) 3177-3183. [PMID: 3319582]
Accepted name: ADP-ribosyl-[dinitrogen reductase] hydrolase
Reaction: ADP-D-ribosyl-[dinitrogen reductase] = ADP-D-ribose + [dinitrogen reductase]
Other name(s): azoferredoxin glycosidase; azoferredoxin-activating enzymes; dinitrogenase reductase-activating glycohydrolase; ADP-ribosyl glycohydrolase
Systematic name: ADP-D-ribosyl-[dinitrogen reductase] ADP-ribosylhydrolase
Comments: Together with EC 2.4.2.37 NAD+—dinitrogen-reductase ADP-D-ribosyltransferase, , this enzyme controls the level of activity of EC 1.18.6.1 nitrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 125626-63-3
References:
1. Fitzmaurice, W.P., Saari, L.L., Lowery, R.G., Ludden, P.W. and Roberts, G.P. Genes coding for the reversible ADP-ribosylation system of dinitrogenase reductase from Rhodospirillum rubrum. Mol. Gen. Genet. 218 (1989) 340-347. [PMID: 2506427]
Accepted name: N-methyl nucleosidase
Reaction: 7-methylxanthosine + H2O = 7-methylxanthine + D-ribose
For diagram of reaction click here
Other name(s): 7-methylxanthosine nucleosidase; N-MeNase; N-methyl nucleoside hydrolase; methylpurine nucleosidase
Systematic name: 7-methylxanthosine ribohydrolase
Comments: The enzyme preferentially hydrolyses 3- and 7-methylpurine nucleosides, such as 3-methylxanthosine, 3-methyladenosine and 7-methylguanosine. Hydrolysis of 7-methylxanthosine to form 7-methylxanthine is the second step in the caffeine-biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1.Negishi, O., Ozawa, T. and Imagawa, H. N-Methyl nucleosidase from tea leaves. Agric. Biol. Chem. 52 (1988) 169-175.
Accepted name: futalosine hydrolase
Reaction: futalosine + H2O = dehypoxanthine futalosine + hypoxanthine
Glossary: futalosine = 3-(3-((3S,4R)-3,4-dihydroxy-5-(6-oxo-3H-purin-9(6H)-yl)tetrahydrofuran-2-yl)propanoyl)benzoate
dehypoxanthine futalosine = 7-(3-carboxyphenyl)-D-ribo-7-dehydro-5,6-dideoxyheptose
Other name(s): futalosine nucleosidase; MqnB
Systematic name: futalosine ribohydrolase
Comments: This enzyme, which is specific for futalosine, catalyses the second step of a novel menaquinone biosynthetic pathway that is found in some prokaryotes.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hiratsuka, T., Furihata, K., Ishikawa, J., Yamashita, H., Itoh, N., Seto, H. and Dairi, T. An alternative menaquinone biosynthetic pathway operating in microorganisms. Science 321 (2008) 1670-1673. [PMID: 18801996]
Accepted name: uracil-DNA glycosylase
Reaction: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil
Other name(s): UdgB (ambiguous); uracil-DNA N-glycosylase; UDG (ambiguous); uracil DNA glycohydrolase
Systematic name: uracil-DNA deoxyribohydrolase (uracil-releasing)
Comments: Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms. EC 3.2.2.27 and double-stranded uracil-DNA glycosylase (EC 3.2.2.28) form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolysing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalysing the removal of mis-incorporated uracil from DNA.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Lee, M.S., Kim, G.A., Seo, M.S., Lee, J.H. and Kwon, S.T. Characterization of heat-labile uracil-DNA glycosylase from Psychrobacter sp. HJ147 and its application to the polymerase chain reaction. Biotechnol. Appl. Biochem. 52 (2009) 167-175. [PMID: 18412541]
2. Kim, G.A., Lee, M.S., Sun, Y., Lee, B.D., Lee, J.I., Lee, J.H. and Kwon, S.T. Characterization of cold-active uracil-DNA glycosylase from Bacillus sp. HJ171 and its use for contamination control in PCR. Appl. Microbiol. Biotechnol. 80 (2008) 785-794. [PMID: 18626641]
3. Parikh, S.S., Putnam, C.D. and Tainer, J.A. Lessons learned from structural results on uracil-DNA glycosylase. Mutat Res 460 (2000) 183-199. [PMID: 10946228]
4. Stivers, J.T. and Drohat, A.C. Uracil DNA glycosylase: insights from a master catalyst. Arch. Biochem. Biophys. 396 (2001) 1-9. [PMID: 11716455]
Accepted name: double-stranded uracil-DNA glycosylase
Reaction: Specifically hydrolyzes mismatched double-stranded DNA and polynucleotides, releasing free uracil
Other name(s): Mug; double-strand uracil-DNA glycosylase; Dug; dsUDG; double-stranded DNA specific UDG; dsDNA specific UDG; UdgB (ambiguous); G:T/U mismatch-specific DNA glycosylase; UDG (ambiguous)
Systematic name: uracil-double-stranded DNA deoxyribohydrolase (uracil-releasing)
Comments: No activity on DNA containing a T/G mispair or single-stranded DNA containing either a site-specific uracil or 3,N4-ethenocytosine residue [2], significant role for double-stranded uracil-DNA glycosylase in mutation avoidance in non-dividing E. coli [3]. Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms. Uracil-DNA glycosylase (EC 3.2.2.27) and EC 3.2.2.28 form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolysing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalysing the removal of mis-incorporated uracil from DNA.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Barrett, T.E., Scharer, O.D., Savva, R., Brown, T., Jiricny, J., Verdine, G.L. and Pearl, L.H. Crystal structure of a thwarted mismatch glycosylase DNA repair complex. EMBO J. 18 (1999) 6599-6609. [PMID: 10581234]
2. Sung, J.S. and Mosbaugh, D.W. Escherichia coli double-strand uracil-DNA glycosylase: involvement in uracil-mediated DNA base excision repair and stimulation of activity by endonuclease IV. Biochemistry 39 (2000) 10224-10235. [PMID: 10956012]
3. Mokkapati, S.K., Fernandez de Henestrosa, A.R. and Bhagwat, A.S. Escherichia coli DNA glycosylase Mug: a growth-regulated enzyme required for mutation avoidance in stationary-phase cells. Mol. Microbiol. 41 (2001) 1101-1111. [PMID: 11555290]
Accepted name: thymine-DNA glycosylase
Reaction: Hydrolyzes mismatched double-stranded DNA and polynucleotides, releasing free thymine
Other name(s): mismatch-specific thymine-DNA glycosylase; mismatch-specific thymine-DNA N-glycosylase; hTDG; hsTDG; TDG; thymine DNA glycosylase; G/T glycosylase; uracil/thymine DNA glycosylase; T:G mismatch-specific thymidine-DNA glycosylase; G:T mismatch-specific thymine DNA-glycosylase
Systematic name: thymine-DNA deoxyribohydrolase (thymine-releasing)
Comments: Thymine-DNA glycosylase is part of the DNA-repair machinery. Thymine removal is fastest when it is from a G/T mismatch with a 5'-flanking C/G pair. The glycosylase removes uracil from G/U, C/U, and T/U base pairs faster than it removes thymine from G/T [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Waters, T.R. and Swann, P.F. Thymine-DNA glycosylase and G to A transition mutations at CpG sites. Mutat Res 462 (2000) 137-147. [PMID: 10767625]
2. Neddermann, P. and Jiricny, J. The purification of a mismatch-specific thymine-DNA glycosylase from HeLa cells. J. Biol. Chem. 268 (1993) 21218-21224. [PMID: 8407958]
3. Waters, T.R. and Swann, P.F. Kinetics of the action of thymine DNA glycosylase. J. Biol. Chem. 273 (1998) 20007-20014. [PMID: 9685338]
[EC 3.2.3.1 Transferred entry: now EC 3.2.1.147 thioglucosidase (EC 3.2.3.1 created 1972, deleted 2001)]