Biology:UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—D-lysine ligase
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Short description: Class of enzymes
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—D-lysine ligase | |||||||||
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Identifiers | |||||||||
EC number | 6.3.2.37 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—D-lysine ligase (EC 6.3.2.37, UDP-MurNAc-L-Ala-D-Glu:D-Lys ligase, D-lysine-adding enzyme) is an enzyme with systematic name UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:D-lysine alpha-ligase (ADP-forming).[1] This enzyme catalyses the following chemical reaction
- ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + D-lysine [math]\displaystyle{ \rightleftharpoons }[/math] ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-D-lysine
The enzyme from Thermotoga maritima also performs the reaction of EC 6.3.2.7.
References
- ↑ "The MurE synthetase from Thermotoga maritima is endowed with an unusual D-lysine adding activity". The Journal of Biological Chemistry 281 (23): 15680–6. June 2006. doi:10.1074/jbc.M506311200. PMID 16595662.
External links
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—D-lysine+ligase at the US National Library of Medicine Medical Subject Headings (MeSH)
Original source: https://en.wikipedia.org/wiki/UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—D-lysine ligase.
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