Entry Name UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---D-lysine ligase;
Class Ligases;BRITE hierarchy
Sysname UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate:D-lysine gamma-ligase (ADP-forming)
Reaction(IUBMB) ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + D-lysine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-Nepsilon-D-lysine [RN:
R09596 ]
Reaction(KEGG) Substrate ATP [CPD:
C00002 ];
UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate [CPD:
C00692 ];
D-lysine [CPD:
C00739 ]
Product ADP [CPD:
C00008 ];
phosphate [CPD:
C00009 ];
UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-Nepsilon-D-lysine
Comment 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.
History EC 6.3.2.37 created 2011, modified 2015
Reference Authors Boniface A, Bouhss A, Mengin-Lecreulx D, Blanot D
Title The MurE synthetase from Thermotoga maritima is endowed with an unusual D-lysine adding activity.
Journal Sequence Other DBs ExplorEnz - The Enzyme Database: 6.3.2.37
ExPASy - ENZYME nomenclature database: 6.3.2.37
