KEGG   ENZYME: 6.3.1.12Help
Entry
EC 6.3.1.12                 Enzyme                                 

Name
D-aspartate ligase;
Aslfm;
UDP-MurNAc-pentapeptide:D-aspartate ligase;
D-aspartic acid-activating enzyme
Class
Ligases;
Forming carbon-nitrogen bonds;
Acid-D-ammonia (or amine) ligases (amide synthases)
BRITE hierarchy
Sysname
D-aspartate:[beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n ligase (ADP-forming)
Reaction(IUBMB)
ATP + D-aspartate + [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n = [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]n + ADP + phosphate [RN:R09590]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
D-aspartate [CPD:C00402];
[beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n [CPD:C19695]
Product
[beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]n [CPD:C19696];
ADP [CPD:C00008];
phosphate [CPD:C00009]
Comment
This enzyme forms part of the peptidoglycan assembly pathway of Gram-positive bacteria grown in medium containing D-Asp. Normally, the side chains the acylate the 6-amino group of the L-lysine residue contain L-Ala-L-Ala but these amino acids are replaced by D-Asp when D-Asp is included in the medium. Hybrid chains containing L-Ala-D-Asp, L-Ala-L-Ala-D-Asp or D-Asp-L-Ala are not formed [4]. The enzyme belongs in the ATP-grasp protein superfamily [3,4]. The enzyme is highly specific for D-aspartate, as L-aspartate, D-glutamate, D-alanine, D-iso-asparagine and D-malic acid are not substrates [4]. In Enterococcus faecium, the substrate D-aspartate is produced by EC 5.1.1.13, aspartate racemase [4]
History
EC 6.3.1.12 created 2006
Orthology
K17810  
D-aspartate ligase
Genes
LSP: 
LGY: 
SIV: 
LLA: 
L93420(yxbA)
LLK: 
LLKF_2494(yxbA)
LLT: 
LLS: 
lilo_2195(yxbA)
LLD: 
LLX: 
LLC: 
LLM: 
LLR: 
LLN: 
LLI: 
LLW: 
LJO: 
LJF: 
LJH: 
LJN: 
LAC: 
LAI: 
LAD: 
LSA: 
LSL: 
LSI: 
LSJ: 
LDB: 
LBU: 
LDE: 
LDL: 
LBR: 
LBK: 
LCA: 
LCB: 
LCZ: 
LCS: 
LCE: 
LCW: 
LCL: 
LGA: 
LRE: 
LRF: 
LRU: 
LRT: 
LRR: 
LHE: 
LHL: 
LHR: 
LHV: 
LHH: 
LFE: 
LFR: 
LFF: 
LRH: 
LGG_02152(yxbA)
LRG: 
LRL: 
LRA: 
LRHK_2161(yxbA)
LRO: 
LRC: 
LCR: 
LAM: 
LAY: 
LBH: 
LBN: 
LKE: 
LPI: 
LPQ: 
LAW: 
PPE: 
PPEN: 
PCE: 
PECL_1167(yxbA)
EFC: 
EFAU: 
EFU: 
EFM: 
EFT: 
EHR: 
ECAS: 
EMU: 
EMQU_1641(carB2)
THL: 
CRN: 
CCT: 
XCE: 
IVA: 
SKE: 
CFL: 
CFI: 
CGA: 
TPY: 
ASG: 
BAD: 
BADL: 
BDE: 
BBI: 
BBP: 
BBF: 
BCOR: 
GVA: 
OLS: 
CGO: 
AEQ: 
BDO: 
IAL: 
 » show all
Taxonomy
Reference
1  [PMID:4262567]
  Authors
Staudenbauer W, Strominger JL.
  Title
Activation of D-aspartic acid for incorporation into peptidoglycan.
  Journal
J. Biol. Chem. 247 (1972) 5095-102.
Reference
2  [PMID:4626717]
  Authors
Staudenbauer W, Willoughby E, Strominger JL.
  Title
Further studies of the D-aspartic acid-activating enzyme of Streptococcus faecalis and its attachment to the membrane.
  Journal
J. Biol. Chem. 247 (1972) 5289-96.
Reference
3  [PMID:9416615]
  Authors
Galperin MY, Koonin EV.
  Title
A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity.
  Journal
Protein. Sci. 6 (1997) 2639-43.
Reference
4  [PMID:16510449]
  Authors
Bellais S, Arthur M, Dubost L, Hugonnet JE, Gutmann L, van Heijenoort J, Legrand R, Brouard JP, Rice L, Mainardi JL.
  Title
Aslfm, the D-aspartate ligase responsible for the addition of D-aspartic acid onto the peptidoglycan precursor of Enterococcus faecium.
  Journal
J. Biol. Chem. 281 (2006) 11586-94.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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