| 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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