| Entry |
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| Name |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---D-lysine ligase;
UDP-MurNAc-L-Ala-D-Glu:D-Lys ligase;
D-lysine-adding enzyme
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| Class |
Ligases;
Forming carbon-nitrogen bonds;
Acid-D-amino-acid ligases (peptide synthases)
 |
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| Sysname |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:D-lysine alpha-ligase (ADP-forming)
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| Reaction(IUBMB) |
ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + D-lysine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-D-lysine [RN: R09596]
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| Reaction(KEGG) |
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| Substrate |
ATP [CPD: C00002];
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate [CPD: C00692];
D-lysine [CPD: C00739]
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| Product |
ADP [CPD: C00008];
phosphate [CPD: C00009];
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-D-lysine [CPD: C19720]
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| Comment |
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. Involved in the synthesis of cell-wall peptidoglycan.
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| Reference |
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| Authors |
Boniface A, Bouhss A, Mengin-Lecreulx D, Blanot D |
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| Title |
The MurE synthetase from Thermotoga maritima is endowed with an unusual D-lysine adding activity. |
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| Journal |
J. Biol. Chem. 281 (2006) 15680-6. |
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| Organism |
Thermotoga maritima [GN: tma] |
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| Sequence |
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| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: |
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