| EC |
6.3.2.9 |
| Accepted name: |
UDP-N-acetylmuramoyl-L-alanine—D-glutamate ligase |
| Reaction: |
ATP + UDP-N-acetyl-α-D-muramoyl-L-alanine + D-glutamate = ADP + phosphate + UDP-N-acetyl-α-D-muramoyl-L-alanyl-D-glutamate |
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For diagram of peptidoglycan biosynthesis (part 1), 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; UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase (ADP-forming) |
| Systematic name: |
UDP-N-acetyl-α-D-muramoyl-L-alanine:D-glutamate ligase (ADP-forming) |
| Comments: |
Involved in the synthesis of a cell-wall peptide in bacteria. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, 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] |
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| [EC 6.3.2.9 created 1965, modified 2002] |
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