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
BACO: OXB_0273
LSP: Bsph_4214
LGY: T479_17810 T479_20575
LFU: HR49_03685 HR49_06090 HR49_17980
LYS: LBYS11_05525 LBYS11_17280 LBYS11_19795
LYB: C3943_20290 C3943_23425
VIL: CFK37_06100
VNE: CFK40_01590
SJE: AAV35_012250
MACR: BHM04_09800
SIV: SSIL_1018
KUR: ASO14_443
LLA: L93420(yxbA)
LLK: LLKF_2494(yxbA)
LLT: CVCAS_2270(yxbA)
LLS: lilo_2195(yxbA)
LLC: LACR_2532
LLM: llmg_2505
LLR: llh_12965
LLW: kw2_2286
LLJ: LG36_2164(yxbA)
LJO: LJ_0136
LJH: LJP_0142
LAC: LBA0159
LAD: LA14_0159
LAF: SD55_0156
LSA: LCA_0098
LSL: LSL_0017
LSI: HN6_00013
LSJ: LSJ_0020
LDB: Ldb0210
LBU: LBUL_0184
LBR: LVIS_1500
LCA: LSEI_2148
LPAP: LBPC_2084
LCB: LCABL_23300(yxbA)
LCS: LCBD_2316
LCE: LC2W_2298
LGA: LGAS_0136
LRE: Lreu_1936
LRF: LAR_1812
LRT: LRI_1883
LHE: lhv_0165
LHL: LBHH_0166
LHV: lhe_0172
LHH: LBH_0137
LHD: HUO_01800
LFE: LAF_1396
LFR: LC40_0892
LFF: LBFF_1517
LRH: LGG_02152(yxbA)
LRG: LRHM_2069
LRL: LC705_02159(yxbA)
LRA: LRHK_2161(yxbA)
LAM: LA2_00865
LBH: Lbuc_1239
LKE: WANG_1714
LAE: LBAT_0182
PPE: PEPE_0661
PPEN: T256_03525
PCE: PECL_1167(yxbA)
EFU: HMPREF0351_11643(carB2)
EFM: M7W_1232
EHR: EHR_10605
ECAS: ECBG_00820
EMU: EMQU_1641(carB2)
EDU: LIU_09540
THL: TEH_12780
CCT: CC1_14460
AMIN: AUMI_17200
LMOI: VV02_09855
XCE: Xcel_1887
CFL: Cfla_1730
CFI: Celf_2121
SERJ: SGUI_1445
TPYO: X956_00020
BAD: BAD_1086
BADL: BADO_1137
BDE: BDP_1523
BDN: BBDE_1447
BBI: BBIF_0602
BBP: BBPR_0578
BBF: BBB_0558
BCOR: BCOR_0477
BANG: BBAG_0555
SIJ: SCIP_0865
PDO: PSDT_0275
AEQ: AEQU_1453
OLS: Olsu_1290
CBAC: JI75_06365
IAL: IALB_2457
 » 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 247:5095-102 (1972)
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 247:5289-96 (1972)
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 6:2639-43 (1997)
DOI:10.1002/pro.5560061218
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 281:11586-94 (2006)
DOI:10.1074/jbc.M600114200
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 6.3.1.12
IUBMB Enzyme Nomenclature: 6.3.1.12
ExPASy - ENZYME nomenclature database: 6.3.1.12
BRENDA, the Enzyme Database: 6.3.1.12

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