EC
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1.1.1.158
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Transferred entry: | UDP-N-acetylmuramate dehydrogenase. Now EC 1.3.1.98, UDP-N-acetylmuramate dehydrogenase
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[EC 1.1.1.158 created 1976, modified 1983, modified 2002, deleted 2013] |
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EC |
1.3.1.98 |
Accepted name: |
UDP-N-acetylmuramate dehydrogenase |
Reaction: |
UDP-N-acetyl-α-D-muramate + NADP+ = UDP-N-acetyl-3-O-(1-carboxyvinyl)-α-D-glucosamine + NADPH + H+ |
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Other name(s): |
MurB reductase; UDP-N-acetylenolpyruvoylglucosamine reductase; UDP-N-acetylglucosamine-enoylpyruvate reductase; UDP-GlcNAc-enoylpyruvate reductase; uridine diphosphoacetylpyruvoylglucosamine reductase; uridine diphospho-N-acetylglucosamine-enolpyruvate reductase; uridine-5′-diphospho-N-acetyl-2-amino-2-deoxy-3-O-lactylglucose:NADP-oxidoreductase |
Systematic name: |
UDP-N-acetyl-α-D-muramate:NADP+ oxidoreductase |
Comments: |
A flavoprotein (FAD). NADH can to a lesser extent replace NADPH. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39307-28-3 |
References: |
1. |
Taku, A. and Anwar, R.A. Biosynthesis of uridine diphospho-N-acetylmuramic acid. IV. Activation of uridine diphospho-N-acetylenolpyruvylglucosamine reductase by monovalent cations. J. Biol. Chem. 248 (1973) 4971. [PMID: 4717533] |
2. |
Taku, A., Gunetileke, K.G. and Anwar, R.A. Biosynthesis of uridine diphospho-N-acetylmuramic acid. 3. Purification and properties of uridine diphospho-N-acetylenolpyruvyl-glucosamine reductase. J. Biol. Chem. 245 (1970) 5012–5016. [PMID: 4394163] |
3. |
van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503–519. [PMID: 11699883] |
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[EC 1.3.1.98 created 1976 as EC 1.1.1.158, modified 1983, modified 2002, transferred 2013 to EC 1.3.1.98] |
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EC
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2.4.1.129
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Transferred entry: | peptidoglycan glycosyltransferase. Now EC 2.4.99.28, peptidoglycan glycosyltransferase
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[EC 2.4.1.129 created 1984, modified 2002, deleted 2023] |
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EC |
2.4.99.28 |
Accepted name: |
peptidoglycan glycosyltransferase |
Reaction: |
[GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate |
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Glossary: |
Mur2Ac = N-acetylmuramic acid |
Other name(s): |
PG-II; bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)-pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D-glucosaminyltransferase; penicillin binding protein (3 or 1B); peptidoglycan transglycosylase; undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide):undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide) disaccharidetransferase |
Systematic name: |
[poly-N-acetyl-D-glucosaminyl-(1→4)-(N-acetyl-D-muramoylpentapeptide)]-diphosphoundecaprenol:[N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide]-diphosphoundecaprenol disaccharidetransferase |
Comments: |
The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here). Involved in the synthesis of cell-wall peptidoglycan. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 79079-04-2 |
References: |
1. |
Taku, A., Stuckey, M. and Fan, D.P. Purification of the peptidoglycan transglycosylase of Bacillus megaterium. J. Biol. Chem. 257 (1982) 5018–5022. [DOI] [PMID: 6802846] |
2. |
Goffin, C. and Ghuysen, J.-M. Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol. Mol. Biol. Rev. 62 (1998) 1079–1093. [DOI] [PMID: 9841666] |
3. |
van Heijenoort, J. Formation of the glycan chains in the synthesis of bacterial peptidoglycan. Glycobiology 11 (2001) 25. [DOI] [PMID: 11320055] |
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[EC 2.4.99.28 created 1984 as EC 2.4.1.129, modified 2002, transferred 2023 to EC 2.4.99.28] |
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EC |
2.5.1.7 |
Accepted name: |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase |
Reaction: |
phosphoenolpyruvate + UDP-N-acetyl-α-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-α-D-glucosamine |
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For diagram of peptidoglycan biosynthesis (part 1), click here |
Other name(s): |
MurA transferase; UDP-N-acetylglucosamine 1-carboxyvinyl-transferase; UDP-N-acetylglucosamine enoylpyruvyltransferase; enoylpyruvate transferase; phosphoenolpyruvate-UDP-acetylglucosamine-3-enolpyruvyltransferase; phosphoenolpyruvate:UDP-2-acetamido-2-deoxy-D-glucose 2-enoyl-1-carboxyethyltransferase; phosphoenolpyruvate:uridine diphosphate N-acetylglucosamine enolpyruvyltransferase; phosphoenolpyruvate:uridine-5′-diphospho-N-acetyl-2-amino-2-deoxyglucose 3-enolpyruvyltransferase; phosphopyruvate-uridine diphosphoacetylglucosamine pyruvatetransferase; pyruvate-UDP-acetylglucosamine transferase; pyruvate-uridine diphospho-N-acetylglucosamine transferase; pyruvate-uridine diphospho-N-acetyl-glucosamine transferase; pyruvic-uridine diphospho-N-acetylglucosaminyltransferase; phosphoenolpyruvate:UDP-N-acetyl-D-glucosamine 1-carboxyvinyltransferase |
Systematic name: |
phosphoenolpyruvate:UDP-N-acetyl-α-D-glucosamine 1-carboxyvinyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9023-27-2 |
References: |
1. |
Gunetileke, K.G. and Anwar, R.A. Biosynthesis of uridine diphospho-N-acetylmuramic acid. II. Purification and properties of pyruvate-uridine diphospho-N-acetylglucosamine transferase and characterization of uridine diphospho-N-acetylenopyruvylglucosamine. J. Biol. Chem. 243 (1968) 5770–5778. [PMID: 5699062] |
2. |
Zemell, R.I. and Anwar, R.A. Pyruvate-uridine diphospho-N-acetylglucosamine transferase. Purification to homogeneity and feedback inhibition. J. Biol. Chem. 250 (1975) 3185–3192. [PMID: 1123336] |
3. |
van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503–519. [PMID: 11699883] |
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[EC 2.5.1.7 created 1972, modified 1983, modified 2002] |
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EC |
2.7.1.170 |
Accepted name: |
anhydro-N-acetylmuramic acid kinase |
Reaction: |
ATP + 1,6-anhydro-N-acetyl-β-muramate + H2O = ADP + N-acetylmuramate 6-phosphate |
Other name(s): |
anhMurNAc kinase; AnmK |
Systematic name: |
ATP:1,6-anhydro-N-acetyl-β-muramate 6-phosphotransferase |
Comments: |
This enzyme, along with EC 4.2.1.126, N-acetylmuramic acid 6-phosphate etherase, is required for the utilization of anhydro-N-acetylmuramic acid in proteobacteria. The substrate is either imported from the medium or derived from the bacterium’s own cell wall murein during cell wall recycling. The product N-acetylmuramate 6-phosphate is produced as a 7:1 mixture of the α- and β-anomers. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Uehara, T., Suefuji, K., Valbuena, N., Meehan, B., Donegan, M. and Park, J.T. Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate. J. Bacteriol. 187 (2005) 3643–3649. [DOI] [PMID: 15901686] |
2. |
Uehara, T., Suefuji, K., Jaeger, T., Mayer, C. and Park, J.T. MurQ etherase is required by Escherichia coli in order to metabolize anhydro-N-acetylmuramic acid obtained either from the environment or from its own cell wall. J. Bacteriol. 188 (2006) 1660–1662. [DOI] [PMID: 16452451] |
3. |
Bacik, J.P., Whitworth, G.E., Stubbs, K.A., Yadav, A.K., Martin, D.R., Bailey-Elkin, B.A., Vocadlo, D.J. and Mark, B.L. Molecular basis of 1,6-anhydro bond cleavage and phosphoryl transfer by Pseudomonas aeruginosa 1,6-anhydro-N-acetylmuramic acid kinase. J. Biol. Chem. 286 (2011) 12283–12291. [DOI] [PMID: 21288904] |
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[EC 2.7.1.170 created 2011, modified 2011] |
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EC |
2.7.1.192 |
Accepted name: |
protein-Nπ-phosphohistidine—N-acetylmuramate phosphotransferase |
Reaction: |
[protein]-Nπ-phospho-L-histidine + N-acetyl-D-muramate[side 1] = [protein]-L-histidine + N-acetyl-D-muramate 6-phosphate[side 2] |
Other name(s): |
murP (gene name); N-acetylmuramic acid PTS permease; EIINAcMur; Enzyme IINAcMur |
Systematic name: |
protein-Nπ-phospho-L-histidine:N-acetyl-D-muramate Nπ-phosphotransferase |
Comments: |
This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Dahl, U., Jaeger, T., Nguyen, B.T., Sattler, J.M. and Mayer, C. Identification of a phosphotransferase system of Escherichia coli required for growth on N-acetylmuramic acid. J. Bacteriol. 186 (2004) 2385–2392. [DOI] [PMID: 15060041] |
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[EC 2.7.1.192 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.192] |
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EC |
2.7.7.99 |
Accepted name: |
N-acetyl-α-D-muramate 1-phosphate uridylyltransferase |
Reaction: |
UDP + N-acetyl-α-D-muramate 1-phosphate = UDP-N-acetyl-α-D-muramate + phosphate |
Glossary: |
N-acetyl-α-D-muramate = 3-O-[(1R)-1-carboxyethyl]-2-acetoxy-2-deoxy-D-glucopyranose |
Other name(s): |
murU (gene name) |
Systematic name: |
UDP:N-acetyl-α-D-muramate 1-phosphate uridylyltransferase |
Comments: |
The enzyme, characterized from Pseudomonas species, participates in a peptidoglycan salvage pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Gisin, J., Schneider, A., Nagele, B., Borisova, M. and Mayer, C. A cell wall recycling shortcut that bypasses peptidoglycan de novo biosynthesis. Nat. Chem. Biol. 9 (2013) 491–493. [DOI] [PMID: 23831760] |
2. |
Renner-Schneck, M., Hinderberger, I., Gisin, J., Exner, T., Mayer, C. and Stehle, T. Crystal structure of the N-acetylmuramic acid α-1-phosphate (MurNAc-α1-P) uridylyltransferase MurU, a minimal sugar nucleotidyltransferase and potential drug target enzyme in Gram-negative pathogens. J. Biol. Chem. 290 (2015) 10804–10813. [DOI] [PMID: 25767118] |
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[EC 2.7.7.99 created 2017] |
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EC |
3.1.3.105 |
Accepted name: |
N-acetyl-D-muramate 6-phosphate phosphatase |
Reaction: |
N-acetyl-D-muramate 6-phosphate + H2O = N-acetyl-D-muramate + phosphate |
Other name(s): |
mupP (gene name) |
Systematic name: |
N-acetyl-D-muramate 6-phosphate phosphohydrolase |
Comments: |
The enzyme, characterized from Pseudomonas species, participates in a peptidoglycan salvage pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Borisova, M., Gisin, J. and Mayer, C. The N-acetylmuramic acid 6-phosphate phosphatase MupP completes the Pseudomonas peptidoglycan recycling pathway leading to intrinsic fosfomycin resistance. mBio 8 (2017) e00092-17. [DOI] [PMID: 28351914] |
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[EC 3.1.3.105 created 2017] |
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EC |
3.2.1.17 |
Accepted name: |
lysozyme |
Reaction: |
Hydrolysis of (1→4)-β-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins |
Other name(s): |
muramidase; globulin G; mucopeptide glucohydrolase; globulin G1; N,O-diacetylmuramidase; lysozyme g; L-7001; 1,4-N-acetylmuramidase; mucopeptide N-acetylmuramoylhydrolase; PR1-lysozyme |
Systematic name: |
peptidoglycan N-acetylmuramoylhydrolase |
Comments: |
cf. also EC 3.2.1.14 chitinase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-63-2 |
References: |
1. |
Blade, C.C.F., Johnson, L.N., Mair, G.A., North, A.C.T., Phillips, D.C. and Sarma, V.R. Crystallographic studies of the activity of hen egg-white lysozyme. Proc. R. Soc. Lond. B: Biol. Sci. 167 (1967) 378–388. [PMID: 4382801] |
2. |
Blake, C.C.F., Mair, G.A., North, A.C.T., Phillips, D.C. and Sarma, V.R. On the conformation of the hen egg-white lysozyme molecule. Proc. R. Soc. Lond. B: Biol. Sci. 167 (1967) 365–377. [PMID: 4382800] |
3. |
Jollès, P. Lysozyme. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 4, Academic Press, New York, 1960, pp. 431–445. |
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[EC 3.2.1.17 created 1961] |
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EC |
3.5.1.28 |
Accepted name: |
N-acetylmuramoyl-L-alanine amidase |
Reaction: |
Hydrolyses the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides |
Glossary: |
thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium |
Other name(s): |
acetylmuramyl-L-alanine amidase; N-acetylmuramyl-L-alanine amidase; N-acylmuramyl-L-alanine amidase; acetylmuramoyl-alanine amidase; N-acetylmuramic acid L-alanine amidase; acetylmuramyl-alanine amidase; N-acetylmuramylalanine amidase; murein hydrolase; N-acetylmuramoyl-L-alanine amidase type I; N-acetylmuramoyl-L-alanine amidase type II |
Systematic name: |
peptidoglycan amidohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9013-25-6 |
References: |
1. |
Ghuysen, J.-M., Dierickx, L., Coyette, J., Leyh-Bouille, M., Guinand, M. and Campbell, J.N. An improved technique for the preparation of Streptomyces peptidases and N-acetylmuramyl-L-alanine amidase active on bacterial wall peptidoglycans. Biochemistry 8 (1969) 213–222. [PMID: 5777325] |
2. |
Herbold, D.R. and Glaser, L. Interaction of N-acetylmuramic acid L-alanine amidase with cell wall polymers. J Biol Chem 250 (1975) 7231–7238. [PMID: 809432] |
3. |
Herbold, D.R. and Glaser, L. Bacillus subtilis N-acetylmuramic acid L-alanine amidase. J. Biol. Chem. 250 (1975) 1676–1682. [PMID: 803507] |
4. |
Ward, J.B., Curtis, C.A.M., Taylor, C. and Buxton, R.S. Purification and characterization of two phage PBSX-induced lytic enzymes of Bacillus subtilis 168: an N-acetylmuramoyl-L-alanine amidase and an N-acetylmuramidase. J. Gen. Microbiol. 128 (1982) 1171–1178. [DOI] [PMID: 6126517] |
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[EC 3.5.1.28 created 1972 (EC 3.4.19.10 created 1992, incorporated 1997)] |
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EC |
4.2.1.126 |
Accepted name: |
N-acetylmuramic acid 6-phosphate etherase |
Reaction: |
(R)-lactate + N-acetyl-D-glucosamine 6-phosphate = N-acetylmuramate 6-phosphate + H2O |
Other name(s): |
MurNAc-6-P etherase; MurQ |
Systematic name: |
(R)-lactate hydro-lyase (adding N-acetyl-D-glucosamine 6-phosphate; N-acetylmuramate 6-phosphate-forming) |
Comments: |
This enzyme, along with EC 2.7.1.170, anhydro-N-acetylmuramic acid kinase, is required for the utilization of anhydro-N-acetylmuramic acid in proteobacteria. The substrate is either imported from the medium or derived from the bacterium’s own cell wall murein during cell wall recycling. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Jaeger, T., Arsic, M. and Mayer, C. Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia coli "etherase". J. Biol. Chem. 280 (2005) 30100–30106. [DOI] [PMID: 15983044] |
2. |
Uehara, T., Suefuji, K., Valbuena, N., Meehan, B., Donegan, M. and Park, J.T. Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate. J. Bacteriol. 187 (2005) 3643–3649. [DOI] [PMID: 15901686] |
3. |
Uehara, T., Suefuji, K., Jaeger, T., Mayer, C. and Park, J.T. MurQ etherase is required by Escherichia coli in order to metabolize anhydro-N-acetylmuramic acid obtained either from the environment or from its own cell wall. J. Bacteriol. 188 (2006) 1660–1662. [DOI] [PMID: 16452451] |
4. |
Hadi, T., Dahl, U., Mayer, C. and Tanner, M.E. Mechanistic studies on N-acetylmuramic acid 6-phosphate hydrolase (MurQ): an etherase involved in peptidoglycan recycling. Biochemistry 47 (2008) 11547–11558. [DOI] [PMID: 18837509] |
5. |
Jaeger, T. and Mayer, C. N-acetylmuramic acid 6-phosphate lyases (MurNAc etherases): role in cell wall metabolism, distribution, structure, and mechanism. Cell. Mol. Life Sci. 65 (2008) 928–939. [DOI] [PMID: 18049859] |
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[EC 4.2.1.126 created 2011] |
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EC |
4.2.2.29 |
Accepted name: |
peptidoglycan lytic transglycosylase |
Reaction: |
a peptidoglycan chain = a peptidoglycan chain with N-acetyl-1,6-anhydromuramyl-(peptide) at the reducing end + a peptidoglycan chain with N-acetylglucosamine at the non-reducing end |
Other name(s): |
lytic murein transglycosylase; endolytic murein transglycosylase; lytic transglycosylase; endolytic transglycosylase; MtlA; MltB; MltC; MltD; MltE; MltF; MltG; Slt; RlpA; SleB; SpoIID |
Systematic name: |
peptidoglycan N-acetylmuramate—N-acetyl-β-D-glucosamine lyase |
Comments: |
A group of bacterial enzymes that catalyse the non-hydrolytic cleavage of peptidoglycan (PG). The enzymes fragment the polysaccharide chain at the β-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine residues by an intramolecular cyclization of the N-acetylmuramyl moiety to yield a 1,6-anhydro-N-acetyl-β-D-muramyl product. Includes endolytic transglycosylase activity that fragments the glycan chain internally and exolytic transgylcosylase activity that cleaves a terminal disaccharide from the end of the glycan strand. The MtlG enzyme of Gram-negative bacteria may function to regulate glycan strand length within the PG polymer. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Holtje, J.V., Mirelman, D., Sharon, N. and Schwarz, U. Novel type of murein transglycosylase in Escherichia coli. J. Bacteriol. 124 (1975) 1067–1076. [DOI] [PMID: 357] |
2. |
Yunck, R., Cho, H. and Bernhardt, T.G. Identification of MltG as a potential terminase for peptidoglycan polymerization in bacteria. Mol. Microbiol. 99 (2016) 700–718. [DOI] [PMID: 26507882] |
3. |
Dik, D.A., Marous, D.R., Fisher, J.F. and Mobashery, S. Lytic transglycosylases: concinnity in concision of the bacterial cell wall. Crit. Rev. Biochem. Mol. Biol. 52 (2017) 503–542. [DOI] [PMID: 28644060] |
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[EC 4.2.2.29 created 2023] |
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EC |
6.3.2.37 |
Accepted name: |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—D-lysine ligase |
Reaction: |
ATP + UDP-N-acetyl-α-D-muramoyl-L-alanyl-D-glutamate + D-lysine = ADP + phosphate + UDP-N-acetyl-α-D-muramoyl-L-alanyl-γ-D-glutamyl-Nε-D-lysine |
Glossary: |
muramic acid = 2-amino-3-O-[(R)-1-carboxyethyl]-2-deoxy-D-glucose |
Other name(s): |
UDP-MurNAc-L-Ala-D-Glu:D-Lys ligase; D-lysine-adding enzyme |
Systematic name: |
UDP-N-acetyl-α-D-muramoyl-L-alanyl-D-glutamate:D-lysine γ-ligase (ADP-forming) |
Comments: |
Involved in the synthesis of cell-wall peptidoglycan. The D-lysine is attached to the peptide chain at the N6 position. The enzyme from Thermotoga maritima also performs the reaction of EC 6.3.2.7, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
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. [DOI] [PMID: 16595662] |
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[EC 6.3.2.37 created 2011, modified 2015] |
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