| EC |
6.3.2.4 |
| Accepted name: |
D-alanine—D-alanine ligase |
| Reaction: |
ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine |
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| 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, Gene, KEGG, MetaCyc, 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. |
| 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 6.3.2.4 created 1961, modified 2002] |
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