Entry
Name
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---L-lysine ligase;
MurE synthetase;
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine synthetase;
uridine diphospho-N-acetylmuramoylalanyl-D-glutamyllysine synthetase;
UPD-MurNAc-L-Ala-D-Glu:L-Lys ligase;
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:L-lysine gamma-ligase (ADP-forming)
Class
Ligases;
Forming carbon-nitrogen bonds;
Acid-D-amino-acid ligases (peptide synthases)
BRITE hierarchy
Sysname
UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate:L-lysine gamma-ligase (ADP-forming)
Reaction(IUBMB)
ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + L-lysine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysine [RN:
R02786 ]
Reaction(KEGG)
Substrate
ATP [CPD:
C00002 ];
UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate [CPD:
C00692 ];
L-lysine [CPD:
C00047 ]
Product
ADP [CPD:
C00008 ];
phosphate [CPD:
C00009 ];
UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysine [CPD:
C05892 ]
Comment
Involved in the synthesis of a cell-wall peptide in bacteria. This enzyme adds lysine in some Gram-positive organisms; in others and in Gram-negative organisms EC
6.3.2.13 (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---2,6-diaminopimelate ligase) adds 2,6-diaminopimelate instead.
History
EC 6.3.2.7 created 1961, modified 2002
Pathway
Orthology
K05362 UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase
Genes
SAX : USA300HOU_0976(murE1)
SUQ : HMPREF0772_12216(murE)
SUX : SAEMRSA15_08480(murE)
SUF : SARLGA251_09330(murE)
SAUV : SAI7S6_1007210(murE)
SAUW : SAI5S5_1007170(murE)
SAUX : SAI6T6_1007180(murE)
SAUY : SAI8T7_1007210(murE)
SDP : NCTC12225_02039(murE)
SPIC : SAMEA4384060_1942(murE)
SSH : NCTC13712_00961(murE)
SSIM : SAMEA4384339_0867(murE)
SSTE : SAMEA4384403_1838(murE)
GMO : NCTC11323_01073(murE)
GHA : NCTC10459_00697(murE)
SPYM : M1GAS476_0392(murE)
SPH : MGAS10270_Spy0320(murE)
SPI : MGAS10750_Spy0321(murE)
SPJ : MGAS2096_Spy0343(murE)
SPK : MGAS9429_Spy0324(murE)
STG : MGAS15252_0351(murE.1)
STX : MGAS1882_0351(murE.1)
STZ : SPYALAB49_000354(murE)
SNV : SPNINV200_13670(murE)
SNC : HMPREF0837_11764(murE)
SPNE : SPN034156_04290(murE)
SPNU : SPN034183_13400(murE)
SPNM : SPN994038_13290(murE)
SPNO : SPN994039_13300(murE)
SMC : SmuNN2025_0440(murE)
SGG : SGGBAA2069_c17290(murE)
SCP : HMPREF0833_10974(murE)
SVB : NCTC12167_00375(murE_1)
SMEN : SAMEA4412692_1073(murE)
SFER : NCTC12278_01481(murE)
SCAI : NCTC12191_00119(murE)
SPSU : NCTC13786_01732(murE)
SPOC : NCTC10925_01423(murE)
SAUP : NCTC3168_01256(murE)
SURN : NCTC13766_01698(murE)
SVF : NCTC3166_01492(murE)
SMIE : NCTC11169_00434(murE)
LGAS : LG045_09270(murE) LG045_09275(murE)
ECEC : NCTC12421_02150(murE)
» show all
Taxonomy
Reference
1
Authors
Ito E, Strominger JL.
Title
Enzymatic synthesis of the peptide in bacterial uridine nucleotides. I. Enzymatic addition of L-alanine, D-glutamic acid, and L-lysine.
Journal
J Biol Chem 237:2689-2695 (1962)
Reference
Authors
van Heijenoort J
Title
Recent advances in the formation of the bacterial peptidoglycan monomer unit.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 6.3.2.7
ExPASy - ENZYME nomenclature database: 6.3.2.7
BRENDA, the Enzyme Database: 6.3.2.7