Continued from EC 6.2.1
EC 6.3.1 Acid—Ammonia (or Amine) Ligases (Amide Synthases)
EC 6.3.2 Acid—Amino-Acid Ligases (Peptide Synthases)
EC 6.3.3 Cyclo-Ligases
EC 6.3.4 Other Carbon—Nitrogen Ligases
EC 6.3.5 Carbon—Nitrogen Ligases with Glutamine as Amido-N-Donor
Accepted name: aspartate—ammonia ligase
Reaction: ATP + L-aspartate + NH3 = AMP + diphosphate + L-asparagine
Other name(s): asparagine synthetase; L-asparagine synthetase
Systematic name: L-aspartate:ammonia ligase (AMP-forming)
Links to other databases: BRENDA, EXPASY, KEGG, PDB, PDB, CAS registry number: 9023-69-2
References:
1. Ravel, J.M., Norton, S.J., Humphreys, J.S. and Shive, W. Asparagine biosynthesis in Lactobacillus arabinosus and its control by asparagine through enzyme inhibition and repression. J. Biol. Chem. 237 (1962) 2845-2849.
2. Webster, G.C. and Varner, J.E. Aspartate metabolism and asparagine synthesis in plant systems. J. Biol. Chem. 215 (1955) 91-99.
Accepted name: glutamate—ammonia ligase
Reaction: ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
Other name(s): glutamine synthetase; glutamylhydroxamic synthetase; L-glutamine synthetase
Systematic name: L-glutamate:ammonia ligase (ADP-forming)
Comments: Also acts, more slowly, on 4-methylene-L-glutamate (cf. EC 6.3.1.7 4-methyleneglutamate—ammonia ligase).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, PDB, PDB, CAS registry number: 9023-70-5
References:
1. Elliott, W.H. Isolation of glutamine synthetase and glutamotransferase from green peas. J. Biol. Chem. 201 (1953) 661-672.
2. Fry, B.A. Glutamine synthesis by Micrococcus pyogenes var. aureus. Biochem. J. 59 (1955) 579-589.
3. Lajtha, A., Mela, P. and Waelsch, H. Manganese-dependent glutamotransferase. J. Biol. Chem. 205 (1953) 553-564.
4. Meister, A. Glutamine synthesis, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 6, Academic Press, New York, 1962, pp. 443-468.
5. Woolfolk, C.A., Shapiro, B. and Stadtman, E.R. Regulation of glutamine synthetase. I. Purification and properties of glutamine synthetase from Escherichia coli. Arch. Biochem. Biophys. 116 (1966) 177-192. [PMID: 5336023]
[EC 6.3.1.3 Transferred entry: now EC 6.3.4.13 phosphoribosylamine—glycine ligase (created 1961, deleted 1972)]
Accepted name: aspartate—ammonia ligase (ADP-forming)
Reaction: ATP + L-aspartate + NH3 = ADP + phosphate + L-asparagine
Other name(s): asparagine synthetase (ADP-forming); asparagine synthetase (adenosine diphosphate-forming)
Systematic name: L-aspartate:ammonia ligase (ADP-forming)
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37318-61-9
References:
1. Nair, P.M. Asparagine synthetase from γ-irradiated potatoes. Arch. Biochem. Biophys. 133 (1969) 208-215. [PMID: 5820987]
Accepted name: NAD+ synthase
Reaction: ATP + deamido-NAD+ + NH3 = AMP + diphosphate + NAD+
Other name(s): NAD synthetase; NAD synthase; nicotinamide adenine dinucleotide synthetase; diphosphopyridine nucleotide synthetase
Systematic name: deamido-NAD+:ammonia ligase (AMP-forming)
Comments: L-Glutamine also acts, more slowly, as amido-donor [cf. EC 6.3.5.1, NAD+ synthase (glutamine-hydrolysing)].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9032-69-3
References:
1. Spencer, R.L. and Preiss, J. Biosynthesis of diphosphopyridine nucleotide. The purification and the properties of diphosphopyridine nucleotide synthetase from Escherichia coli B. J. Biol. Chem. 242 (1967) 385-392. [PMID: 4290215]
Accepted name: glutamate—ethylamine ligase
Reaction: ATP + L-glutamate + ethylamine = ADP + phosphate + N5-ethyl-L-glutamine
Other name(s): N5-ethyl-L-glutamine synthetase; theanine synthetase; N5-ethylglutamine synthetase
Systematic name: L-glutamate:ethylamine ligase (ADP-forming)
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 62213-31-4
References:
1. Sasaoka, K. and Kito, M. Synthesis of theanine by tea seedling homogenate. Agric. Biol. Chem. 28 (1964) 313-317.
2. Sasaoka, K., Kito, M. and Inagaki, H. Studies on the biosynthesis of theanine in tea seedlings. Synthesis of theanine by the homogenate of tea seedlings. Agric. Biol. Chem. 27 (1963) 467-468.
3. Sasaoka, K., Kito, M. and Onishi, Y. Some properties of the theanine synthesizing enzyme in tea seedlings. Agric. Biol. Chem. 29 (1965) 984-988.
Accepted name: 4-methyleneglutamate—ammonia ligase
Reaction: ATP + 4-methylene-L-glutamate + NH3 = AMP + diphosphate + 4-methylene-L-glutamine
Other name(s): 4-methyleneglutamine synthetase
Systematic name: 4-methylene-L-glutamate:ammonia ligase (AMP-forming)
Comments: Glutamine can act instead of NH3, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 85537-85-5
References:
1. Winter, H.C., Su, T.-Z. and Dekker, E.E. 4-Methyleneglutamine synthetase: a new amide synthetase present in germinating peanuts. Biochem. Biophys. Res. Commun. 111 (1983) 484-489. [PMID: 6838571]
Accepted name: glutathionylspermidine synthase
Reaction: glutathione + spermidine + ATP = glutathionylspermidine + ADP + phosphate
For diagram click here.
Glossary: glutathione = γ-L-glutamyl-L-cysteinyl-glycine
spermidine
Other name(s): glutathione:spermidine ligase (ADP-forming)
Systematic name: γ-L-Glutamyl-L-cysteinyl-glycine:spermidine ligase (ADP-forming) [spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule]
Comments: Requires magnesium ions. Involved in the synthesis of trypanothione in trypanosomatids. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine amidase (EC 3.5.1.78) reaction, resulting in a net hydrolysis of ATP.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9077-09-2
References:
1. Smith, K., Nadeau, K., Bradley, M., Walsh, C.T., Fairlamb, A.H. Purification of glutathionylspermidine and trypanothione synthase from Crithidia fasciculata. Protein Sci. 1 (1992) 874-883. [PMID: 1304372]
2. 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 glutathionyl spermidine synthetase/amidase. J. Biol. Chem. 270 (1995) 14031-14041. [PMID: 7775463]
Accepted name: trypanothione synthase
Reaction: glutathione + glutathionylspermidine + ATP = N1,N8-bis(glutathionyl)spermidine + ADP + phosphate
For diagram click here.
Systematic name: glutathionylspermidine:glutathione ligase (ADP-forming)
Comments: involved in the synthesis of trypanothione in trypanosomatids
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 130246-69-4
References:
1. Smith, K., Nadeau, K., Bradley, M., Walsh, C.T., Fairlamb, A.H. Purification of glutathionyl spermidine and trypanothione synthase from Crithidia fasciculata. Protein Sci. 1 (1992) 874-883. [PMID: 1304372]
Accepted name: adenosylcobinamide-phosphate synthase
Reaction: (1) ATP + adenosylcobyric acid + (R)-1-aminopropan-2-yl phosphate = ADP + phosphate + adenosylcobinamide phosphate
(2) ATP + adenosylcobyric acid + (R)-1-aminopropan-2-ol = ADP + phosphate + adenosylcobinamide
For diagram click here.
Other name(s): CbiB
Systematic name: adenosylcobyric acid:(R)-1-aminopropan-2-yl phosphate ligase (ADP-forming)
Comments: One of the substrates for this reaction, (R)-1-aminopropan-2-yl phosphate, is produced by CobD (EC 4.1.1.81, threonine-phosphate decarboxylase).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 905988-16-1
References:
1. Cheong, C.G., Bauer, C.B., Brushaber, K.R., Escalante-Semerena, J.C. and Rayment, I. Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica. Biochemistry 41 (2002) 4798-4808. [PMID: 11939774]
2. Warren, M.J., Raux, E., Schubert, H.L. and Escalante-Semerena, J.C. The biosynthesis of adenosylcobalamin (vitamin B12). Nat. Prod. Rep. 19 (2002) 390-412. [PMID: 12195810]
Accepted name: glutamate—putrescine ligase
Reaction: ATP + L-glutamate + putrescine = ADP + phosphate + γ-L-glutamylputrescine
Other name(s): γ-glutamylputrescine synthetase; YcjK
Systematic name: L-glutamate:putrescine ligase (ADP-forming)
Comments: Forms part of a novel bacterial putrescine utilization pathway in Escherichia coli.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 914090-78-1
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: D-aspartate ligase
Reaction: ATP + D-aspartate + [β-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]n = [β-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-6-N-(β-D-Asp)-L-Lys-D-Ala-D-Ala)]n + ADP + phosphate
For diagram click here.
Other name(s): Aslfm; UDP-MurNAc-pentapeptide:D-aspartate ligase; D-aspartic acid-activating enzyme
Systematic name: D-aspartate:[β-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]n ligase (ADP-forming)
Comments: This enzyme forms part of the peptidoglycan assembly pathway of Gram-positive bacteria grown in medium containing D-Asp. Normally, the side chains the acylate the 6-amino group of the L-lysine residue contain L-Ala-L-Ala but these amino acids are replaced by D-Asp when D-Asp is included in the medium. Hybrid chains containing L-Ala-D-Asp, L-Ala-L-Ala-D-Asp or D-Asp-L-Ala are not formed [4]. The enzyme belongs in the ATP-grasp protein superfamily [3,4]. The enzyme is highly specific for D-aspartate, as L-aspartate, D-glutamate, D-alanine, D-iso-asparagine and D-malic acid are not substrates [4]. In Enterococcus faecium, the substrate D-aspartate is produced by EC 5.1.1.13, aspartate racemase [4]
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Staudenbauer, W. and Strominger, J.L. Activation of D-aspartic acid for incorporation into peptidoglycan. J. Biol. Chem. 247 (1972) 5095-5102. [PMID: 4262567]
2. Staudenbauer, W., Willoughby, E. and Strominger, J.L. Further studies of the D-aspartic acid-activating enzyme of Streptococcus faecalis and its attachment to the membrane. J. Biol. Chem. 247 (1972) 5289-5296. [PMID: 4626717]
3. Galperin, M.Y. and Koonin, E.V. A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. Protein Sci. 6 (1997) 2639-2643. [PMID: 9416615]
4. Bellais, S., Arthur, M., Dubost, L., Hugonnet, J.E., Gutmann, L., van Heijenoort, J., Legrand, R., Brouard, J.P., Rice, L. and Mainardi, J.L. Aslfm, the D-aspartate ligase responsible for the addition of D-aspartic acid onto the peptidoglycan precursor of Enterococcus faecium. J. Biol. Chem. 281 (2006) 11586-11594. [PMID: 16510449]
Accepted name: L-cysteine:1D-myo-inositol 2-amino-2-deoxy-α-D-glucopyranoside ligase
Reaction: 1-O-(2-amino-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol + L-cysteine + ATP = 1-O-[2-(L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol + AMP + diphosphate
Glossary: mycothiol = 1-O-[2-(N2-acetyl-L-cysteinamido)-2-deoxy--D-glucopyranosyl]-1D-myo-inositol
Other name(s): MshC; MshC ligase; Cys:GlcN-Ins ligase; mycothiol ligase
Systematic name: L-cysteine:1-O-(2-amino-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol ligase (AMP-forming)
Comments: This enzyme is a key enzyme in the biosynthesis of mycothiol, a small molecular weight thiol found in Mycobacteria spp. and other actinomycetes. Mycothiol plays a fundamental role in these organisms by helping to provide protection from the effects of reactive oxygen species and electrophiles, including many antibiotics. The enzyme may represent a novel target for new classes of antituberculars [2]
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Fan, F., Luxenburger, A., Painter, G.F. and Blanchard, J.S. Steady-state and pre-steady-state kinetic analysis of Mycobacterium smegmatis cysteine ligase (MshC). Biochemistry 46 (2007) 11421-11429. [PMID: 17848100]
2. Gutierrez-Lugo, M.T., Newton, G.L., Fahey, R.C. and Bewley, C.A. Cloning, expression and rapid purification of active recombinant mycothiol ligase as B1 immunoglobulin binding domain of streptococcal protein G, glutathione-S-transferase and maltose binding protein fusion proteins in Mycobacterium smegmatis. Protein Expr. Purif. 50 (2006) 128-136. [PMID: 16908186]
3. Tremblay, L.W., Fan, F., Vetting, M.W. and Blanchard, J.S. The 1.6 Å crystal structure of Mycobacterium smegmatis MshC: the penultimate enzyme in the mycothiol biosynthetic pathway. Biochemistry 47 (2008) 13326-13335. [PMID: 19053270]
Accepted name: diphthine—ammonia ligase
Reaction: ATP + diphthine + NH3 = ADP + phosphate + diphthamide
Other name(s): diphthamide synthase; diphthamide synthetase
Systematic name: diphthine:ammonia ligase (ADP-forming)
Comments: This amidase catalyses the last step in the conversion of an L-histidine residue in the translation elongation factor eEF-2 to diphthamide. This factor is found in all archaebacteria and eukaryotes, but not in eubacteria, and is the target of bacterial toxins such as the diphtheria toxin and the Pseudomonas exotoxin A (see EC 2.4.2.36, NAD+—diphthamide ADP-ribosyltransferase). The substrate of the enzyme, diphthine, is produced by EC 2.1.1.98, diphthine synthase. The nature of the ammonia donor is not known.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Moehring, J.M. and Moehring, T.J. The post-translational trimethylation of diphthamide studied in vitro. J. Biol. Chem. 263 (1988) 3840-3844. [PMID: 3346227]
2. Moehring, T.J. and Moehring, J.M. Mutant cultured cells used to study the synthesis of diphthamide. UCLA Symp. Mol. Cell. Biol. New Ser. 45 (1987) 53-63.
Accepted name: pantoate—β-alanine ligase
Reaction: ATP + (R)-pantoate + β-alanine = AMP + diphosphate + (R)-pantothenate
For diagram of reaction click here.
Other name(s): pantothenate synthetase; pantoate activating enzyme; pantoic-activating enzyme; D-pantoate:β-alanine ligase (AMP-forming)
Systematic name: (R)-pantoate:β-alanine ligase (AMP-forming)
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9023-49-8
References:
1. Ginoza, H.S. and Altenbern, R.A. The pantothenate-synthesizing enzyme cell-free extracts of Brucella abortus, strain 19. Arch. Biochem. Biophys. 56 (1955) 537-541.
2. Maas, W.K. Pantothenate studies. III. Description of the extracted pantothenate-synthesizing enzyme of Escherichia coli. J. Biol. Chem. 198 (1952) 23-32.
3. Maas, W.K. Mechanism of the enzymatic synthesis of pantothenate from beta-alanine and pantoate. Fed. Proc. 15 (1956) 305-306.
Accepted name: glutamate—cysteine ligase
Reaction: ATP + L-glutamate + L-cysteine = ADP + phosphate + γ-L-glutamyl-L-cysteine
Other name(s): γ-glutamylcysteine synthetase; γ-glutamyl-L-cysteine synthetase; γ-glutamylcysteinyl synthetase
Systematic name: L-glutamate:L-cysteine γ-ligase (ADP-forming)
Comments: Can use L-aminohexanoate in place of glutamate.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9023-64-7
References:
1. Mackinnon, C.M., Carter, P.E., Smyth, S.J., Dunbar, B. and Fothergill, J.E. Molecular-cloning of cDNA for human-complement component c1s - the complete amino-acid sequence. Eur. J. Biochem. 169 (1987) 547-553.
2. Snoke, J.E., Yanari, S. and Bloch, K. Synthesis of glutathione from γ-glutamylcysteine. J. Biol. Chem. 201 (1953) 573-586.
3. Mandeles, S. and Bloch, K. Enzymatic synthesis of γ-glutamylcysteine. J. Biol. Chem. 214 (1955) 639-646.
Accepted name: glutathione synthase
Reaction: ATP + γ-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
Other name(s): glutathione synthetase; GSH synthetase
Systematic name: γ-L-glutamyl-L-cysteine:glycine ligase (ADP-forming)
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9023-62-5
References:
1. Law, M.Y. and Halliwell, B. Purification and properties of glutathione synthetase from (Spinacia oleracea) leaves. Plant Sci. 43 (1986) 185-191.
2. Macnicol, P.K. Homoglutathione and glutathione synthetases of legume seedlings - partial-purification and substrate-specificity. Plant Sci. 53 (1987) 229-235.
Accepted name: D-alanine—D-alanine ligase
Reaction: ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine
For diagram click here.
Other name(s): MurE synthetase [ambiguous]; alanine:alanine ligase (ADP-forming); alanylalanine synthetase
Systematic name: D-alanine:D-alanine ligase (ADP-forming)
Comments: Involved with EC 6.3.2.7 (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase) or EC 6.3.2.13 (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate ligase), EC 6.3.2.8 (UDP-N-acetylmuramate—L-alanine ligase), EC 6.3.2.9 (UDP-N-acetylmuramoyl-L-alanine—D-glutamate ligase) and EC 6.3.2.10 (UDP-N-acetylmuramoyl-tripeptide—D-alanyl-D-alanine ligase) in the synthesis of a cell-wall peptide (click here for diagram).
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9023-63-6
References:
1. Ito, E. and Strominger, J.L. Enzymatic synthesis of the peptide in bacterial uridine nucleotides. II. Enzymatic synthesis and addition of D-alanyl-D-alanine. J. Biol. Chem. 237 (1962) 2696-2703.
2. Neuhaus, F.C. Kinetic studies on D-Ala-D-Ala synthetase. Fed. Proc. 21 (1962) 229 only.
3. van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503-519. [PMID: 11699883]
Accepted name: phosphopantothenate—cysteine ligase
Reaction: CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
For diagram click here.
Other name(s): phosphopantothenoylcysteine synthetase
Systematic name: (R)-4'-phosphopantothenate:L-cysteine ligase
Comments: Cysteine can be replaced by some of its derivatives.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9023-50-1
References:
1. Brown, G.M. The metabolism of pantothenic acid. J. Biol. Chem. 234 (1959) 370-378.
2. Strauss, E., Kinsland, C., Ge, Y., McLafferty, F.W. and Begley, T.P. Phosphopantothenoylcysteine synthetase from Escherichia coli. Identification and characterization of the last unidentified Coenzyme A biosynthetic enzymes in bacteria. J. Biol. Chem. 276 (2001) 13513-13516. [PMID: 11278255]
3. Kupke, T. Molecular characterization of the 4'-phosphopantothenoylcysteine synthetase domain of bacterial Dfp flavoproteins. J. Biol. Chem. 277 (2002) 36137-36145. [PMID: 12140293]
Accepted name: phosphoribosylaminoimidazolesuccinocarboxamide synthase
Reaction: ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
For diagram, click here
Other name(s): phosphoribosylaminoimidazole-succinocarboxamide synthetase; PurC; SAICAR synthetase; 4-(N-succinocarboxamide)-5-aminoimidazole synthetase; 4-[(N-succinylamino)carbonyl]-5-aminoimidazole ribonucleotide synthetase; SAICARs; 5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase; phosphoribosylaminoimidazolesuccinocarboxamide synthetase; 5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase
Systematic name: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate:L-aspartate ligase (ADP-forming)
Comments: Forms part of the purine biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9023-67-0
References:
1. Lukens, L.N. and Buchanan, J.M. Biosynthesis of purines. XXIV. The enzymatic synthesis of 5-amino-1-ribosyl-4-imidazolecarboxylic acid 5'-phosphate from 5-amino-1-ribosylimidazole 5'-phosphate and carbon dioxide. J. Biol. Chem. 234 (1959) 1799-1805. [PMID: 13672967]
2. Parker, J. Identification of the purC gene product of Escherichia coli. J. Bacteriol. 157 (1984) 712-717. [PMID: 6365889]
3. Ebbole, D.J. and Zalkin, H. Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis. J. Biol. Chem. 262 (1987) 8274-8287. [PMID: 3036807]
4. Chen, Z.D., Dixon, J.E. and Zalkin, H. Cloning of a chicken liver cDNA encoding 5-aminoimidazole ribonucleotide carboxylase and 5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase by functional complementation of Escherichia coli pur mutants. Proc. Natl. Acad. Sci. USA 87 (1990) 3097-3101. [PMID: 1691501]
5. O'Donnell, A.F., Tiong, S., Nash, D. and Clark, D.V. The Drosophila melanogaster ade5 gene encodes a bifunctional enzyme for two steps in the de novo purine synthesis pathway. Genetics 154 (2000) 1239-1253. [PMID: 10757766]
6. Nelson, S.W., Binkowski, D.J., Honzatko, R.B. and Fromm, H.J. Mechanism of action of Escherichia coli phosphoribosylaminoimidazolesuccinocarboxamide synthetase. Biochemistry 44 (2005) 766-774. [PMID: 15641804]
Accepted name: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase
Reaction: ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine
For diagram click here.
Other name(s): MurE synthetase; UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine synthetase; uridine diphospho-N-acetylmuramoylalanyl-D-glutamyllysine synthetase; UPD-MurNAc-L-Ala-D-Glu:L-Lys ligase
Systematic name: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:L-lysine γ-ligase (ADP-forming)
Comments: Involved with EC 6.3.2.4 (D-alanine—D-alanine ligase), EC 6.3.2.8 (UDP-N-acetylmuramate—L-alanine ligase), EC 6.3.2.9 (UDP-N-acetylmuramoyl-L-alanine—D-glutamate ligase) and EC 6.3.2.10 (UDP-N-acetylmuramoyl-tripeptide—D-alanyl-D-alanine ligase) in the synthesis of a cell-wall peptide (click here for diagram). This enzyme adds lysine in some Gram-positive organisms; in others and in Gram-negative organisms EC 6.3.2.13 (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate ligase) adds 2,6-diaminopimelate instead.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9023-51-2
References:
1. Ito, E. and Strominger, J.L. Enzymatic synthesis of the peptide in bacterial uridine nucleotides. I. Enzymatic addition of L-alanine, D-glutamic acid, and L-lysine. J. Biol. Chem. 237 (1962) 2689-2695.
2. van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503-519. [PMID: 11699883]
Accepted name: UDP-N-acetylmuramate—L-alanine ligase
Reaction: ATP + UDP-N-acetylmuramate + L-alanine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine
For diagram click here.
Other name(s): MurC synthetase; UDP-N-acetylmuramoyl-L-alanine synthetase; uridine diphospho-N-acetylmuramoylalanine synthetase; UDP-N-acetylmuramoylalanine synthetase; L-alanine-adding enzyme; UDP-acetylmuramyl-L-alanine synthetase; UDPMurNAc-L-alanine synthetase; L-Ala ligase; uridine diphosphate N-acetylmuramate:L-alanine ligase; uridine 5'-diphosphate-N-acetylmuramyl-L-alanine synthetase; uridine-diphosphate-N-acetylmuramate:L-alanine ligase; UDP-MurNAc:L-alanine ligase; alanine-adding enzyme; UDP-N-acetylmuramyl:L-alanine ligase
Systematic name: UDP-N-acetylmuramate:L-alanine ligase (ADP-forming)
Comments: Involved with EC 6.3.2.4 (D-alanine—D-alanine ligase), EC 6.3.2.7 (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase) or EC 6.3.2.13 (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate ligase), EC 6.3.2.9 (UDP-N-acetylmuramoyl-L-alanine—D-glutamate ligase) and EC 6.3.2.10 (UDP-N-acetylmuramoyl-tripeptide—D-alanyl-D-alanine ligase) in the synthesis of a cell-wall peptide (click here for diagram).
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9023-52-3
References:
1. Ito, E. and Strominger, J.L. Enzymatic synthesis of the peptide in bacterial uridine nucleotides. I. Enzymatic addition of L-alanine, D-glutamic acid, and L-lysine. J. Biol. Chem. 237 (1962) 2689-2695.
2. Nathenson, S.G., Strominger, J.L. and Ito, E. Enzymatic synthesis of the peptide in bacterial uridine nucleotides. IV. Purification and properties of D-glutamic acid-adding enzyme. J. Biol. Chem. 239 (1964) 1773-1776.
3. van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503-519. [PMID: 11699883]
Accepted name: UDP-N-acetylmuramoyl-L-alanine—D-glutamate ligase
Reaction: ATP + UDP-N-acetylmuramoyl-L-alanine + D-glutamate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
For diagram click here.
Other name(s): MurD synthetase; UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; uridine diphospho-N-acetylmuramoylalanyl-D-glutamate synthetase; D-glutamate-adding enzyme; D-glutamate ligase; UDP-Mur-NAC-L-Ala:D-Glu ligase; UDP-N-acetylmuramoyl-L-alanine:glutamate ligase (ADP-forming); UDP-N-acetylmuramoylalanine—D-glutamate ligase
Systematic name: UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase (ADP-forming)
Comments: Involved with EC 6.3.2.4 (D-alanine—D-alanine ligase), EC 6.3.2.7 (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase) or EC 6.3.2.13 (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate ligase), EC 6.3.2.8 (UDP-N-acetylmuramate—L-alanine ligase) and EC 6.3.2.10 (UDP-N-acetylmuramoyl-tripeptide—D-alanyl-D-alanine ligase) in the synthesis of a cell-wall peptide (click here for diagram).
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9023-59-0
References:
1. Ito, E. and Strominger, J.L. Enzymatic synthesis of the peptide in bacterial uridine nucleotides. I. Enzymatic addition of L-alanine, D-glutamic acid, and L-lysine. J. Biol. Chem. 237 (1962) 2689-2695.
2. van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503-519. [PMID: 11699883]
Accepted name: UDP-N-acetylmuramoyl-tripeptide—D-alanyl-D-alanine ligase
Reaction: ATP + UDP-N-acetylmuramoyl-L-alanyl-γ-D-glutamyl-L-lysine + D-alanyl-D-alanine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-γ-D-glutamyl-L-lysyl-D-alanyl-D-alanine
For diagram click here.
Other name(s): MurF synthetase; UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine synthetase; UDP-N-acetylmuramoylalanyl-D-glutamyl-lysine-D-alanyl-D-alanine ligase; uridine diphosphoacetylmuramoylpentapeptide synthetase; UDPacetylmuramoylpentapeptide synthetase; UDP-MurNAc-L-Ala-D-Glu-L-Lys:D-Ala-D-Ala ligase
Systematic name: UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine:D-alanyl-D-alanine ligase (ADP-forming)
Comments: Involved with EC 6.3.2.4 (D-alanine—D-alanine ligase), EC 6.3.2.7 (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase) or EC 6.3.2.13 (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate ligase), EC 6.3.2.8 (UDP-N-acetylmuramate—L-alanine ligase) and EC 6.3.2.9 (UDP-N-acetylmuramoyl-L-alanine—D-glutamate ligase) in the synthesis of a cell-wall peptide (click here for diagram). This enzyme also catalyses the reaction when the C-terminal residue of the tripeptide is meso-2,4-diaminoheptanedioate (acylated at its L-centre), linking the D-Ala-D-Ala to the carboxy group of the L-centre. This activity was previously attributed to EC 6.3.2.15, which has since been deleted.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 55354-36-4
References:
1. Ito, E. and Strominger, J.L. Enzymatic synthesis of the peptide in bacterial uridine nucleotides. II. Enzymatic synthesis and addition of D-alanyl-D-alanine. J. Biol. Chem. 237 (1962) 2696-2703.
2. van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503-519. [PMID: 11699883]
Accepted name: carnosine synthase
Reaction: ATP + L-histidine + β-alanine = ADP + phosphate + carnosine
Glossary: carnosine = N-β-alanyl-L-histidine
Other name(s): carnosine synthetase; carnosine-anserine synthetase; homocarnosine-carnosine synthetase; carnosine-homocarnosine synthetase; L-histidine:β-alanine ligase (AMP-forming) (incorrect)
Systematic name: L-histidine:β-alanine ligase (ADP-forming)
Comments: This enzyme was thought to form AMP [1,2], but studies with highly purified enzyme proved that it forms ADP [4]. Carnosine is a dipeptide that is present at high concentrations in skeletal muscle and the olfactory bulb of vertebrates [3]. It is also found in the skeletal muscle of some invertebrates. The enzyme can also catalyse the formation of homocarnosine from 4-aminobutanoate and L-histidine, with much lower activity [4].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9023-61-4
References:
1. Kalyankar, G.D. and Meister, A. Enzymatic synthesis of carnosine and related β-alanyl and γ-aminobutyryl peptides. J. Biol. Chem. 234 (1959) 3210-3218. [PMID: 14404206]
2. Stenesh, J.J. and Winnick, T. Carnosine-anserine synthetase of muscle. 4. Partial purification of the enzyme and further studies of β-alanyl peptide synthesis. Biochem. J. 77 (1960) 575-581. [PMID: 16748858]
3. Crush, K.G. Carnosine and related substances in animal tissues. Comp. Biochem. Physiol. 34 (1970) 3-30. [PMID: 4988625]
4. Drozak, J., Veiga-da-Cunha, M., Vertommen, D., Stroobant, V. and Van Schaftingen, E. Molecular identification of carnosine synthase as ATP-grasp domain-containing protein 1 (ATPGD1). J. Biol. Chem. 285 (2010) 9346-9356. [PMID: 20097752]
Accepted name: dihydrofolate synthase
Reaction: ATP + 7,8-dihydropteroate + L-glutamate = ADP + phosphate + 7,8-dihydropteroylglutamate
For diagram click here.
Other name(s): dihydrofolate synthetase; 7,8-dihydrofolate synthetase; H2-folate synthetase; 7,8-dihydropteroate:L-glutamate ligase (ADP); dihydrofolate synthetase-folylpolyglutamate synthetase; folylpoly-(γ-glutamate) synthetase-dihydrofolate synthase; FHFS; FHFS/FPGS; dihydropteroate:L-glutamate ligase (ADP-forming); DHFS
Systematic name: 7,8-dihydropteroate:L-glutamate ligase (ADP-forming)
Comments: In some bacteria, a single protein catalyses both this activity and that of EC 6.3.2.17, tetrahydrofolate synthase [2], the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H4PteGlun), i.e. various tetrahydrofolates. In contrast, the activities are located on separate proteins in most eukaryotes studied to date [3]. This enzyme is reponsible for attaching the first glutamate residue to dihydropteroate to form dihydrofolate and is present only in those organisms that have the ability to synthesize tetrahydrofolate de novo, e.g. plants, most bacteria, fungi and protozoa [3].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37318-62-0
References:
1. Griffin, M.J. and Brown, G.M. The biosynthesis of folic acid. III. Enzymatic formation of dihydrofolic acid from dihydropteroic acid and of tetrahydropteroylpolyglutamic acid compounds from tetrahydrofolic acid. J. Biol. Chem. 239 (1964) 310-316. [PMID: 14114858]
2. Bognar, A.L., Osborne, C., Shane, B., Singer, S.C. and Ferone, R. Folylpoly-γ-glutamate synthetase-dihydrofolate synthetase. Cloning and high expression of the Escherichia coli folC gene and purification and properties of the gene product. J. Biol. Chem. 260 (1985) 5625-5630. [PMID: 2985605]
3. Ravanel, S., Cherest, H., Jabrin, S., Grunwald, D., Surdin-Kerjan, Y., Douce, R. and Rébeillé, F. Tetrahydrofolate biosynthesis in plants: molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 98 (2001) 15360-15365. [PMID: 11752472]
4. Cherest, H., Thomas, D. and Surdin-Kerjan, Y. Polyglutamylation of folate coenzymes is necessary for methionine biosynthesis and maintenance of intact mitochondrial genome in Saccharomyces cerevisiae. J. Biol. Chem. 275 (2000) 14056-14063. [PMID: 10799479]
5. Cossins, E.A. and Chen, L. Folates and one-carbon metabolism in plants and fungi. Phytochemistry 45 (1997) 437-452. [PMID: 9190084]
Accepted name: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate ligase
Reaction: ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-γ-glutamyl-meso-2,6-diaminoheptanedioate
For diagram of reaction, (click here.
Other name(s): MurE synthetase [ambiguous]; UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-2,6-diamino-heptanedioate ligase (ADP-forming); UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelate synthetase; UDP-N-acetylmuramoylalanyl-D-glutamate—2,6-diaminopimelate ligase
Systematic name: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-2,6-diaminoheptanedioate γ-ligase (ADP-forming)
Comments: Involved with EC 6.3.2.4 (D-alanine—D-alanine ligase), EC 6.3.2.8 (UDP-N-acetylmuramate—L-alanine ligase), EC 6.3.2.9 (UDP-N-acetylmuramoyl-L-alanine—D-glutamate ligase) and EC 6.3.2.10 (UDP-N-acetylmuramoyl-tripeptide—D-alanyl-D-alanine ligase) in the synthesis of a cell-wall peptide (click here for diagram). This enzyme adds diaminopimelate in Gram-negative organisms and in some Gram-positive organisms; in others EC 6.3.2.7 (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase) adds lysine instead. It is the amino group of the L-centre of the diaminopimelate that is acylated.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9075-09-6
References:
1. Mizuno, Y. and Ito, E. Purification and properties of uridine diphosphate N-acetylmuramyl-L-alanyl-D-glutamate:meso-2,6-diaminopimelate ligase. J. Biol. Chem. 243 (1968) 2665-2672. [PMID: 4967958]
2. van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503-519. [PMID: 11699883]
Accepted name: 2,3-dihydroxybenzoate—serine ligase
Reaction: ATP + 2,3-dihydroxybenzoate + L-serine = products of ATP breakdown + N-(2,3-dihydroxybenzoyl)-L-serine
Other name(s): N-(2,3-dihydroxybenzoyl)-serine synthetase; 2,3-dihydroxybenzoylserine synthetase
Systematic name: 2,3-dihydroxybenzoate:L-serine ligase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37318-63-1
References:
1. Brot, N. and Goodwin, J. Regulation of 2,3-dihydroxybenzoylserine synthetase by iron. J. Biol. Chem. 243 (1968) 510-513. [PMID: 4966114]
[EC 6.3.2.15 Deleted entry: UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine ligase. The activity observed is due to EC 6.3.2.10, UDP-N-acetylmuramoyl-tripeptide—D-alanyl-D-alanine ligase. (EC 6.3.2.15 created 1976, deleted 2002)]
Accepted name: D-alanine—alanyl-poly(glycerolphosphate) ligase
Reaction: ATP + D-alanine + alanyl-poly(glycerolphosphate) = ADP + phosphate + D-alanyl-alanyl-poly(glycerolphosphate)
Other name(s): D-alanyl-alanyl-poly(glycerolphosphate) synthetase; D-alanine:membrane-acceptor ligase; D-alanylalanylpoly(phosphoglycerol) synthetase; D-alanyl-poly(phosphoglycerol) synthetase; D-alanine-membrane acceptor-ligase
Systematic name: D-alanine:alanyl-poly(glycerolphosphate) ligase (ADP-forming)
Comments: Involved in the synthesis of teichoic acids.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9046-58-6
References:
1. Reusch, V.M. and Neuhaus, F.C. D-Alanine: membrane acceptor ligase from Lactobacillus casei. J. Biol. Chem. 246 (1971) 6136-6143. [PMID: 4399593]
Accepted name: tetrahydrofolate synthase
Reaction: ATP + tetrahydropteroyl-[γ-Glu]n + L-glutamate = ADP + phosphate + tetrahydropteroyl-[γ-Glu]n+1
For diagram click here.
Other name(s): folylpolyglutamate synthase; folate polyglutamate synthetase; formyltetrahydropteroyldiglutamate synthetase; N10-formyltetrahydropteroyldiglutamate synthetase; folylpoly-γ-glutamate synthase; folylpolyglutamyl synthetase; folylpoly(γ-glutamate) synthase; folylpolyglutamate synthetase; folylpoly-γ-glutamate synthetase-dihydrofolate synthetase; FPGS; tetrahydrofolylpolyglutamate synthase; tetrahydrofolate:L-glutamate γ-ligase (ADP-forming); tetrahydropteroyl-[γ-Glu]n:L-glutamate γ-ligase (ADP-forming)
Systematic name: tetrahydropteroyl-γ-polyglutamate:L-glutamate γ-ligase (ADP-forming)
Comments: In some bacteria, a single protein catalyses both this activity and that of EC 6.3.2.12, dihydrofolate synthase [3], the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H4PteGlun), i.e. various tetrahydrofolates (H4folate). In contrast, the activities are located on separate proteins in most eukaryotes studied to date [4]. In Arabidopsis thaliana, this enzyme is present as distinct isoforms in the mitochondria, the cytosol and the chloroplast. Each isoform is encoded by a separate gene, a situation that is unique among eukaryotes [4]. As the affinity of folate-dependent enzymes increases markedly with the number of glutamic residues, the tetrahydropteroyl polyglutamates are the preferred coenzymes of C1 metabolism. (reviewed in [5]). The enzymes from different sources (particularly eukaryotes versus prokaryotes) have different substrate specificities with regard to one-carbon substituents and the number of glutamate residues present on the tetrahydrofolates.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 63363-84-8
References:
1. Cichowicz, D., Foo, S.K. and Shane, B. Folylpoly-γ-glutamate synthesis by bacteria and mammalian cells. Mol. Cell. Biochem. 39 (1981) 209-228. [PMID: 6458762]
2. McGuire, J.J. and Bertino, J.R. Enzymatic synthesis and function of folylpolyglutamates. Mol. Cell. Biochem. 38 (1981) 19-48. [PMID: 7027025]
3. Bognar, A.L., Osborne, C., Shane, B., Singer, S.C. and Ferone, R. Folylpoly-γ-glutamate synthetase-dihydrofolate synthetase. Cloning and high expression of the Escherichia coli folC gene and purification and properties of the gene product. J. Biol. Chem. 260 (1985) 5625-5630. [PMID: 2985605]
4. Ravanel, S., Cherest, H., Jabrin, S., Grunwald, D., Surdin-Kerjan, Y., Douce, R. and Rébeillé, F. Tetrahydrofolate biosynthesis in plants: molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 98 (2001) 15360-15365. [PMID: 11752472]
5. Cossins, E.A. and Chen, L. Folates and one-carbon metabolism in plants and fungi. Phytochemistry 45 (1997) 437-452. [PMID: 9190084]
6. Cherest, H., Thomas, D. and Surdin-Kerjan, Y. Polyglutamylation of folate coenzymes is necessary for methionine biosynthesis and maintenance of intact mitochondrial genome in Saccharomyces cerevisiae. J. Biol. Chem. 275 (2000) 14056-14063. [PMID: 10799479 ]
Accepted name: γ-glutamylhistamine synthase
Reaction: ATP + L-glutamate + histamine = products of ATP breakdown + Nα-γ-L-glutamylhistamine
Other name(s): γ-glutaminylhistamine synthetase; γ-GHA synthetase
Systematic name: L-glutamate:histamine ligase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 82904-08-3
References:
1. Stein, C. and Weinreich, D. An in vitro characterization of γ-glutamylhistamine synthetase: a novel enzyme catalyzing histamine metabolism in the central nervous system of the marine mollusk, Aplysia californica. J. Neurochem. 38 (1982) 204-214. [PMID: 6125565]
Accepted name: ubiquitin—protein ligase
Reaction: ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine
Other name(s): ubiquitin-activating enzyme
Systematic name: ubiquitin:protein-lysine N-ligase (AMP-forming)
Comments: Ubiquitin is coupled to protein by a peptide bond between the C-terminal glycine of ubiquitin and ε-amino groups of lysine residues in the protein. An intermediate in the reaction contains one ubiquitin residue bound as a thioester to the enzyme, and a residue of ubiquitin adenylate non-covalently bound to the enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 74812-49-0
References:
1. Ciechanover, A., Elias, S., Heller, H. and Hershko, A. "Covalent affinity" purification of ubiquitin-activating enzyme. J. Biol. Chem. 257 (1982) 2537-2542. [PMID: 6277904]
2. Haas, A.L. and Rose, I.A. The mechanism of ubiquitin activating enzyme. A kinetic and equilibrium analysis. J. Biol. Chem. 257 (1982) 10329-10337. [PMID: 6286650]
3. Haas, A.L., Warms, J.V.B., Hershko, A. and Rose, I.A. Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation. J. Biol. Chem. 257 (1982) 2543-2548. [PMID: 6277905]
4. Hershko, A., Heller, H., Eytan, E. and Reiss, Y. The protein substrate binding site of the ubiquitin-protein ligase system. J. Biol. Chem. 261 (1986) 11992-11999. [PMID: 3017957]
Accepted name: indoleacetate—lysine synthetase
Reaction: ATP + (indol-3-yl)acetate + L-lysine = ADP + phosphate + N6-[(indole-3-yl)acetyl]-L-lysine
Other name(s): indoleacetate:L-lysine ligase (ADP-forming)
Systematic name: (indol-3-yl)acetate:L-lysine ligase (ADP-forming)
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 103537-15-1
References:
1. Glass, N.L. and Kosuge, T. Cloning of the gene for indoleacetic acid-lysine synthetase from Pseudomonas syringae subsp. savastanoi. J. Bacteriol. 166 (1986) 598. [PMID: 3084452]
2. Hutzinger, O. and Kosuge, T. Microbial synthesis and degradation of indole-3-acetic acid. 3. The isolation and characterization of indole-3-acetyl-ε-L-lysine. Biochemistry 7 (1968) 601-605. [PMID: 5644130]
Accepted name: ubiquitin—calmodulin ligase
Reaction: n ATP + calmodulin + n ubiquitin = n AMP + n diphosphate + (ubiquitin)n-calmodulin
Other name(s): ubiquityl-calmodulin synthase; ubiquitin-calmodulin synthetase; ubiquityl-calmodulin synthetase; uCaM-synthetase
Systematic name: calmodulin:ubiquitin ligase (AMP-forming)
Comments: Specific for Ca2+-calmodulin from vertebrates. At least three ubiquitin molecules can be coupled to lysine residues in calmodulin.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 119632-60-9
References:
1. Jennissen, H.P. and Laub, M. Ubiquitin-calmodulin conjugating activity from cardiac muscle. Biol. Chem. Hoppe-Seyler 369 (1988) 1325-1330. [PMID: 2853950]
2. Ziegenhagen, R. and Jennissen, H.P. Multiple ubiquitination of vertebrate calmodulin by reticulocyte lysate and inhibition of calmodulin conjugation by phosphorylase kinase. Biol. Chem. Hoppe-Seyler 369 (1988) 1317-1324. [PMID: 2853949]
[EC 6.3.2.22 Transferred entry: diphthine—ammonia ligase. Now EC 6.3.1.14, diphthine—ammonia ligase. (EC 6.3.2.22 created 1990, deleted 2010)]
Accepted name: homoglutathione synthase
Reaction: ATP + γ-L-glutamyl-L-cysteine + β-alanine = ADP + phosphate + γ-L-glutamyl-L-cysteinyl-β-alanine
Other name(s): homoglutathione synthetase; β-alanine specific hGSH synthetase
Systematic name: γ-L-glutamyl-L-cysteine:β-alanine ligase (ADP-forming)
Comments: Not identical with EC 6.3.2.3 glutathione synthase.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 113875-72-2
References:
1. Macnicol, P.K. Homoglutathione and glutathione synthetases of legume seedlings - partial-purification and substrate-specificity. Plant Sci. 53 (1987) 229-235.
Accepted name: tyrosine—arginine ligase
Reaction: ATP + L-tyrosine + L-arginine = AMP + diphosphate + L-tyrosyl-L-arginine
Other name(s): tyrosyl-arginine synthase; kyotorphin synthase; kyotorphin-synthesizing enzyme; kyotorphin synthetase
Systematic name: L-tyrosine:L-arginine ligase (AMP-forming)
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 116036-78-3
References:
1. Ueda, H., Yoshihara, Y., Fukushima, N., Shiomi, H., Nakamura, A. and Takagi, H. Kyotorphin (tyrosine-arginine) synthetase in rat brain synaptosomes. J. Biol. Chem. 262 (1987) 8165-8173. [PMID: 3597366]
Accepted name: tubulin—tyrosine ligase
Reaction: ATP + detyrosinated α-tubulin + L-tyrosine = α-tubulin + ADP + phosphate
Systematic name: α-tubulin:L-tyrosine ligase (ADP-forming)
Comments: L-Tyrosine is linked via a peptide bond to the C-terminus of de-tyrosinated α-tubulin (des-Tyrω-α-tubulin). The enzyme is highly specific for α-tubulin and moderately specific for ATP and L-tyrosine. L-Phenylalanine and 3,4-dihydroxy-L-phenylalanine are transferred but with higher Km values.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 60321-03-1
References:
1. Wehland, J., Schröder, H.C., Weber, K. Isolation and purification of tubulin-tyrosine ligase. Methods Enzymol. 134 (1986) 170-179. [PMID: 3821560]
2. Rudiger, M., Wehland, J., Weber, K. The carboxy-terminal peptide of detyrosinated alpha tubulin provides a minimal system to study the substrate specificity of tubulin-tyrosine ligase. Eur. J. Biochem. 220 (1994) 309-320. [PMID: 7510228]
Accepted name: N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase
Reaction: 3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O = 3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
For diagram click here and possible mechanism click here.
Other name(s): L-δ-(α-aminoadipoyl)-L-cysteinyl-D-valine synthetase; ACV synthetase; L-α-aminoadipyl-cysteinyl-valine synthetase
Systematic name: L-2-aminohexanedioate:L-cysteine:L-valine ligase (AMP-forming, valine-inverting)
Comments: Requires Mg2+. The enzyme contains 4'-phosphopantetheine, which may be involved in the mechanism of the reaction. Forms part of the penicillin biosynthesis pathway (for pathway, click here).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 57219-73-5
References:
1. Byford, M.F., Baldwin, J.E., Shiau, C.-Y. and Schofield, C.J. The mechanism of ACV synthetase. Chem. Rev. 97 (1997) 2631-2649. [PMID: 11851475]
2. Theilgaard, H.B., Kristiansen, K.N., Henriksen, C.M. and Nielsen, J. Purification and characterization of δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine synthetase from Penicillium chrysogenum. Biochem. J. 327 (1997) 185-191. [PMID: 9355751]
Accepted name: aerobactin synthase
Reaction: 4 ATP + citrate + 2 N6-acetyl-N6-hydroxy-L-lysine + 2 H2O = 4 ADP + 4 phosphate + aerobactin
For diagram, click here
Systematic name: citrate:N6-acetyl-N6-hydroxy-L-lysine ligase (ADP-forming)
Comments: Requires Mg2+. Aerobactin is one of a group of high-affinity iron chelators known as siderophores and is produced under conditions of iron deprivation [5]. It is a dihydroxamate comprising two molecules of N6-acetyl-N6-hydroxylysine and one molecule of citric acid. This is the last of the three enzymes involved in its synthesis, the others being EC 1.14.13.59, L-lysine 6-monooxygenase (NADPH) and EC 2.3.1.102, N6-hydroxylysine O-acetyltransferase [3].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 94047-30-0
References:
1. Appanna, D.L., Grundy, B.J., Szczepan, E.W. and Viswanatha, T. Aerobactin synthesis in a cell-free system of Aerobacter aerogenes 62-1. Biochim. Biophys. Acta 801 (1984) 437-443.
2. Gibson, F. and Magrath, D.I. The isolation and characterization of a hydroxamic acid (aerobactin) formed by Aerobacter aerogenes 62-I. Biochim. Biophys. Acta 192 (1969) 175-184. [PMID: 4313071]
3. Maurer, P.J. and Miller, M. Microbial iron chelators: total synthesis of aerobactin and its constituent amino acid, N6-acetyl-N6-hydroxylysine. J. Am. Chem. Soc. 104 (1982) 3096-3101.
4. de Lorenzo, V., Bindereif, A., Paw, B.H. and Neilands, J.B. Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12. J. Bacteriol. 165 (1986) 570-578. [PMID: 2935523]
5. Challis, G.L. A widely distributed bacterial pathway for siderophore biosynthesis independent of nonribosomal peptide synthetases. ChemBioChem 6 (2005) 601-611. [PMID: 15719346]
Accepted name: L-amino-acid α-ligase
Reaction: ATP + an L-amino acid + an L-amino acid = ADP + phosphate + L-aminoacyl-L-amino acid
Other name(s): L-amino acid α-ligase; bacilysin synthetase; YwfE; L-amino acid ligase
Systematic name: L-amino acid:L-amino acid ligase (ADP-forming)
Comments: The enzyme from Bacillus sp. requires Mg2+ or Mn2+ for activity. While the enzyme has extremely broad substrate specificity, it does not accept highly charged amino acids, such as Lys, Arg, Glu and Asp, nor does it react with secondary amines such as Pro. The N-terminal residue of the α-dipeptide formed seems to be limited to Ala, Gly, Ser, Thr and Met (with Ala and Ser being the most preferred), whereas the C-terminal residue seems to allow for a wider variety of amino acids (but with a preference for Met and Phe). However, not all combinations or dipeptides are formed. For example, while Ser is acceptable for the N-terminus and Thr for the C-terminus, a Ser-Thr dipeptide is not formed. D-Ala, D-Ser and D-Phe are not substrates. Belongs in the ATP-dependent carboxylate-amine/thiol ligase superfamily.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 939985-65-6
References:
1. Tabata, K., Ikeda, H. and Hashimoto, S. ywfE in Bacillus subtilis codes for a novel enzyme, L-amino acid ligase. J. Bacteriol. 187 (2005) 5195-5202. [PMID: 16030213]
Accepted name: cyanophycin synthase (L-aspartate-adding)
Reaction: ATP + [L-Asp(4-L-Arg)]n + L-Asp = ADP + phosphate + [L-Asp(4-L-Arg)]n—L-Asp
For diagram click here.
Glossary: cyanophycin = [L-Asp(4-L-Arg)]n = N-β-aspartylarginine = [L-4-(L-arginin-2-N-yl)aspartic acid]n = poly{N4-[(1S)-1-carboxy-4-guanidinobutyl]-L-asparagine}
Other name(s): CphA (ambiguous); CphA1 (ambiguous); CphA2 (ambiguous); cyanophycin synthetase (ambiguous); multi-L-arginyl-poly-L-aspartate synthase (ambiguous)
Systematic name: cyanophycin:L-aspartate ligase (ADP-forming)
Comments: Requires Mg2+ for activity. Both this enzyme and EC 6.3.2.30, cyanophycin synthase (L-arginine-adding), are required for the elongation of cyanophycin, which is a protein-like cell inclusion that is unique to cyanobacteria and acts as a temporary nitrogen store [2]. Both enzymes are found in the same protein but have different active sites [2,4]. Both L-Asp and L-Arg must be present before either enzyme will display significant activity [2].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Aboulmagd, E., Oppermann-Sanio, F.B. and Steinbüchel, A. Molecular characterization of the cyanophycin synthetase from Synechocystis sp. strain PCC6308. Arch. Microbiol. 174 (2000) 297-306. [PMID: 11131019]
2. Aboulmagd, E., Oppermann-Sanio, F.B. and Steinbüchel, A. Purification of Synechocystis sp. strain PCC6308 cyanophycin synthetase and its characterization with respect to substrate and primer specificity. Appl. Environ. Microbiol. 67 (2001) 2176-2182. [PMID: 11319097]
3. Allen, M.M., Hutchison, F. and Weathers, P.J. Cyanophycin granule polypeptide formation and degradation in the cyanobacterium Aphanocapsa 6308. J. Bacteriol. 141 (1980) 687-693. [PMID: 6767688]
4. Berg, H., Ziegler, K., Piotukh, K., Baier, K., Lockau, W. and Volkmer-Engert, R. Biosynthesis of the cyanobacterial reserve polymer multi-L-arginyl-poly-L-aspartic acid (cyanophycin): mechanism of the cyanophycin synthetase reaction studied with synthetic primers. Eur. J. Biochem. 267 (2000) 5561-5570. [PMID: 10951215]
5. Ziegler, K., Deutzmann, R. and Lockau, W. Cyanophycin synthetase-like enzymes of non-cyanobacterial eubacteria: characterization of the polymer produced by a recombinant synthetase of Desulfitobacterium hafniense. Z. Naturforsch. [C] 57 (2002) 522-529. [PMID: 12132696]
6. Ziegler, K., Diener, A., Herpin, C., Richter, R., Deutzmann, R. and Lockau, W. Molecular characterization of cyanophycin synthetase, the enzyme catalyzing the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin). Eur. J. Biochem. 254 (1998) 154-159. [PMID: 9652408]
Accepted name: cyanophycin synthase (L-arginine-adding)
Reaction: ATP + [L-Asp(4-L-Arg)]n—L-Asp + L-Arg = ADP + phosphate + [L-Asp(4-L-Arg)]n+1
For diagram click here.
Glossary: cyanophycin = [L-Asp(4-L-Arg)]n = N-β-aspartylarginine = [L-4-(L-arginin-2-N-yl)aspartic acid]n = poly{N4-[(1S)-1-carboxy-4-guanidinobutyl]-L-asparagine}
Other name(s): CphA (ambiguous); CphA1 (ambiguous); CphA2 (ambiguous); cyanophycin synthetase (ambiguous); multi-L-arginyl-poly-L-aspartate synthase (ambiguous)
Systematic name: cyanophycin:L-arginine ligase (ADP-forming)
Comments: Requires Mg2+ for activity. Both this enzyme and EC 6.3.2.29, cyanophycin synthase (L-aspartate-adding), are required for the elongation of cyanophycin, which is a protein-like cell inclusion that is unique to cyanobacteria and acts as a temporary nitrogen store [2]. Both enzymes are found in the same protein but have different active sites [2,4]. Both L-Asp and L-Arg must be present before either enzyme will display significant activity [2]. Canavanine and lysine can be incoporated into the polymer instead of arginine [2].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Aboulmagd, E., Oppermann-Sanio, F.B. and Steinbüchel, A. Molecular characterization of the cyanophycin synthetase from Synechocystis sp. strain PCC6308. Arch. Microbiol. 174 (2000) 297-306. [PMID: 11131019]
2. Aboulmagd, E., Oppermann-Sanio, F.B. and Steinbüchel, A. Purification of Synechocystis sp. strain PCC6308 cyanophycin synthetase and its characterization with respect to substrate and primer specificity. Appl. Environ. Microbiol. 67 (2001) 2176-2182. [PMID: 11319097]
3. Allen, M.M., Hutchison, F. and Weathers, P.J. Cyanophycin granule polypeptide formation and degradation in the cyanobacterium Aphanocapsa 6308. J. Bacteriol. 141 (1980) 687-693. [PMID: 6767688]
4. Berg, H., Ziegler, K., Piotukh, K., Baier, K., Lockau, W. and Volkmer-Engert, R. Biosynthesis of the cyanobacterial reserve polymer multi-L-arginyl-poly-L-aspartic acid (cyanophycin): mechanism of the cyanophycin synthetase reaction studied with synthetic primers. Eur. J. Biochem. 267 (2000) 5561-5570. [PMID: 10951215]
5. Ziegler, K., Deutzmann, R. and Lockau, W. Cyanophycin synthetase-like enzymes of non-cyanobacterial eubacteria: characterization of the polymer produced by a recombinant synthetase of Desulfitobacterium hafniense. Z. Naturforsch. [C] 57 (2002) 522-529. [PMID: 12132696]
6. Ziegler, K., Diener, A., Herpin, C., Richter, R., Deutzmann, R. and Lockau, W. Molecular characterization of cyanophycin synthetase, the enzyme catalyzing the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin). Eur. J. Biochem. 254 (1998) 154-159. [PMID: 9652408]
Accepted name: coenzyme F420-0:L-glutamate ligase
Reaction: GTP + coenzyme F420-0 + L-glutamate = GDP + phosphate + coenzyme F420-1
For diagram of reaction, click here
Glossary: coenzyme F420
Other name(s): CofE-AF; MJ0768; CofE
Systematic name: L-glutamate:coenzyme F420-0 ligase (GDP-forming)
Comments: This protein catalyses the successive addition of two glutamate residues to cofactor F420 by two distinct and independent reactions. In the reaction described here the enzyme attaches a glutamate via its α-amine group to F420-0. In the second reaction (EC 6.3.2.34, coenzyme F420-1—γ-L-glutamate ligase) it catalyses the addition of a second L-glutamate residue to the γ-carboxyl of the first glutamate.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Li, H., Graupner, M., Xu, H. and White, R.H. CofE catalyzes the addition of two glutamates to F420-0 in F420 coenzyme biosynthesis in Methanococcus jannaschii. Biochemistry 42 (2003) 9771-9778. [PMID: 12911320]
2. Nocek, B., Evdokimova, E., Proudfoot, M., Kudritska, M., Grochowski, L.L., White, R.H., Savchenko, A., Yakunin, A.F., Edwards, A. and Joachimiak, A. Structure of an amide bond forming F420:γ-glutamyl ligase from Archaeoglobus fulgidus — a member of a new family of non-ribosomal peptide synthases. J. Mol. Biol. 372 (2007) 456-469. [PMID: 17669425]
Accepted name: coenzyme γ-F420-2:α-L-glutamate ligase
Reaction: ATP + coenzyme γ-F420-2 + L-glutamate = ADP + phosphate + coenzyme α-F420-3
For diagram of reaction, click here
Other name(s): MJ1001; CofF protein; γ-F420-2:α-L-glutamate ligase
Systematic name: L-glutamate:coenzyme γ-F420-2 (ADP-forming)
Comments: The enzyme caps the γ-glutamyl tail of the hydride carrier coenzyme F420 [1].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Li, H., Xu, H., Graham, D.E. and White, R.H. Glutathione synthetase homologs encode α-L-glutamate ligases for methanogenic coenzyme F420 and tetrahydrosarcinapterin biosyntheses. Proc. Natl. Acad. Sci. USA 100 (2003) 9785-9790. [PMID: 12909715]
Accepted name: tetrahydrosarcinapterin synthase
Reaction: ATP + tetrahydromethanopterin + L-glutamate = ADP + phosphate + 5,6,7,8-tetrahydrosarcinapterin
Other name(s): H4MPT:α-L-glutamate ligase; MJ0620; MptN protein
Systematic name: tetrahydromethanopterin:α-L-glutamate ligase (ADP-forming)
Comments: This enzyme catalyses the biosynthesis of 5,6,7,8-tetrahydrosarcinapterin, a modified form of tetrahydromethanopterin found in the Methanosarcinales. It does not require K+, and does not discriminate between ATP and GTP [1].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Li, H., Xu, H., Graham, D.E. and White, R.H. Glutathione synthetase homologs encode α-L-glutamate ligases for methanogenic coenzyme F420 and tetrahydrosarcinapterin biosyntheses. Proc. Natl. Acad. Sci. USA 100 (2003) 9785-9790. [PMID: 12909715]
Accepted name: coenzyme F420-1:γ-L-glutamate ligase
Reaction: GTP + coenzyme F420-1 + L-glutamate = GDP + phosphate + coenzyme γ-F420-2
For diagram of reaction, click here
Glossary: coenzyme F420
Other name(s): F420:γ-glutamyl ligase; CofE-AF; MJ0768; CofE
Systematic name: L-glutamate:coenzyme F420-1 ligase (GDP-forming)
Comments: This protein catalyses the successive addition of two glutamate residues to cofactor F420 by two distinct and independent reactions. In the first reaction (EC 6.3.2.31, coenzyme F420-0—L-glutamate ligase) the enzyme attaches a glutamate via its α-amine group to F420-0. In the second reaction, which is described here, the enzyme catalyses the addition of a second L-glutamate residue to the γ-carboxyl of the first glutamate.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Li, H., Graupner, M., Xu, H. and White, R.H. CofE catalyzes the addition of two glutamates to F420-0 in F420 coenzyme biosynthesis in Methanococcus jannaschii. Biochemistry 42 (2003) 9771-9778. [PMID: 12911320]
2. Nocek, B., Evdokimova, E., Proudfoot, M., Kudritska, M., Grochowski, L.L., White, R.H., Savchenko, A., Yakunin, A.F., Edwards, A. and Joachimiak, A. Structure of an amide bond forming F420:γ-glutamyl ligase from Archaeoglobus fulgidus — a member of a new family of non-ribosomal peptide synthases. J. Mol. Biol. 372 (2007) 456-469. [PMID: 17669425]
Accepted name: D-alanine—D-serine ligase
Reaction: D-alanine + D-serine + ATP = D-alanyl-D-serine + ADP + phosphate
Other name(s): VanC; VanE; VanG
Systematic name: D-alanine:D-serine ligase (ADP-forming)
Comments: The product of this enzyme, D-alanyl-D-serine, can be incorporated into the peptidoglycan pentapeptide instead of the usual D-alanyl-D-alanine dipeptide, which is formed by EC 6.3.2.4, D-alanine—D-alanine ligase. The resulting peptidoglycan does not bind the glycopeptide antibiotics vancomycin and teicoplanin, conferring resistance on the bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Dutka-Malen, S., Molinas, C., Arthur, M. and Courvalin, P. Sequence of the vanC gene of Enterococcus gallinarum BM4174 encoding a D-alanine:D-alanine ligase-related protein necessary for vancomycin resistance. Gene 112 (1992) 53-58. [PMID: 1551598]
2. Park, I.S., Lin, C.H. and Walsh, C.T. Bacterial resistance to vancomycin: overproduction, purification, and characterization of VanC2 from Enterococcus casseliflavus as a D-Ala-D-Ser ligase. Proc. Natl. Acad. Sci. USA 94 (1997) 10040-10044. [PMID: 9294159]
3. Fines, M., Perichon, B., Reynolds, P., Sahm, D.F. and Courvalin, P. VanE, a new type of acquired glycopeptide resistance in Enterococcus faecalis BM4405. Antimicrob. Agents Chemother. 43 (1999) 2161-2164. [PMID: 10471558]
4. Depardieu, F., Bonora, M.G., Reynolds, P.E. and Courvalin, P. The vanG glycopeptide resistance operon from Enterococcus faecalis revisited. Mol. Microbiol. 50 (2003) 931-948. [PMID: 14617152]
5. Watanabe, S., Kobayashi, N., Quinones, D., Hayakawa, S., Nagashima, S., Uehara, N. and Watanabe, N. Genetic Diversity of the Low-Level Vancomycin Resistance Gene vanC-2/vanC-3 and Identification of a Novel vanC Subtype (vanC-4) in Enterococcus casseliflavus. Microb. Drug Resist. 15 (2009) 1-9. [PMID: 19216682]
Accepted name: 4-phosphopantoate—β-alanine ligase
Reaction: ATP + (R)-4-phosphopantoate + β-alanine = AMP + diphosphate + (R)-4'-phosphopantothenate
Other name(s): phosphopantothenate synthetase; TK1686 protein
Systematic name: (R)-4-phosphopantoate:β-alanine ligase (AMP-forming)
Comments: The conversion of (R)-pantoate to (R)-4'-phosphopantothenate is part of the pathway leading to biosynthesis of 4'-phosphopantetheine, an essential cofactor of coenzyme A and acyl-carrier protein. In bacteria and eukaryotes this conversion is performed by condensation with β-alanine, followed by phosphrylation (EC 6.3.2.1 [pantoate—β-alanine ligase] and EC 2.7.1.33 [pantothenate kinase], respectively). In archaea the order of these two steps is reversed, and phosphorylation precedes condensation with β-alanine. The two archaeal enzymes that catalyse this conversion are EC 2.7.1.169, pantoate kinase, and this enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Yokooji, Y., Tomita, H., Atomi, H. and Imanaka, T. Pantoate kinase and phosphopantothenate synthetase, two novel enzymes necessary for CoA biosynthesis in the Archaea. J. Biol. Chem. 284 (2009) 28137-28145. [PMID: 19666462]
Accepted name: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—D-lysine ligase
Reaction: ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + D-lysine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-D-lysine
Other name(s): UDP-MurNAc-L-Ala-D-Glu:D-Lys ligase; D-lysine-adding enzyme
Systematic name: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:L-lysine α-ligase (ADP-forming)
Comments: The enzyme from Thermotoga maritima also performs the reaction of EC 6.3.2.7, UDP-N-acetylmuramoyl-L-alanyl-D-glutamateÐL-lysine ligase. Involved in the synthesis of cell-wall peptidoglycan.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Boniface, A., Bouhss, A., Mengin-Lecreulx, D. and Blanot, D. The MurE synthetase from Thermotoga maritima is endowed with an unusual D-lysine adding activity. J. Biol. Chem. 281 (2006) 15680-15686. [PMID: 16595662]