Entry
Name
aspartate---tRNAAsn ligase;
nondiscriminating aspartyl-tRNA synthetase
Class
Ligases;
Forming carbon-oxygen bonds;
Ligases forming aminoacyl-tRNA and related compounds
BRITE hierarchy
Sysname
L-aspartate:tRNAAsx ligase (AMP-forming)
Reaction(IUBMB)
ATP + L-aspartate + tRNAAsx = AMP + diphosphate + L-aspartyl-tRNAAsx [RN:
R03647 R05577 ]
Reaction(KEGG)
Substrate
Product
AMP [CPD:
C00020 ];
diphosphate [CPD:
C00013 ];
L-aspartyl-tRNAAsx
Comment
When this enzyme acts on tRNAAsp, it catalyses the same reaction as EC
6.1.1.12 , aspartate---tRNA ligase. It has, however, diminished discrimination, so that it can also form aspartyl-tRNAAsn. This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon [1]. This accounts for the ability of this enzyme in, for example, Thermus thermophilus, to recognize both tRNAAsp (GUC anticodon) and tRNAAsn (GUU anticodon). The aspartyl-tRNAAsn is not used in protein synthesis until it is converted by EC
6.3.5.6 , asparaginyl-tRNA synthase (glutamine-hydrolysing), into asparaginyl-tRNAAsn.
History
EC 6.1.1.23 created 2002
Pathway
ec00970 Aminoacyl-tRNA biosynthesis
Orthology
K09759 nondiscriminating aspartyl-tRNA synthetase
Genes
BCG : BCG9842_B3128(aspS1)
BTHU : YBT1518_11975(aspC)
CAC : CA_C2979(aspC) CA_C3564(aspC)
CAE : SMB_G3015(aspS) SMB_G3605(aspC)
CAY : CEA_G2986(aspC1) CEA_G3571(aspC3)
CSR : Cspa_c31980(aspS2) Cspa_c35300(aspS3)
CPAS : Clopa_0265 Clopa_0516
CPAE : CPAST_c01800(aspS1)
CACE : CACET_c24180(aspS2)
CRW : CROST_009700(aspS2_1) CROST_044660(aspS2_2)
CFB : CLFE_003440(aspS2_1) CLFE_039170(aspS2_2)
CAUN : CLAUR_019590(aspS2_1) CLAUR_030410(aspS2_2)
CGEL : psyc5s11_20700(aspC_1)
CTAG : LL095_02340(aspS) LL095_04945(aspS)
CINT : HZF06_01260(aspS) HZF06_04085(aspS)
BPRO : PMF13cell1_01447(aspS2)
BLUI : Blut17040_10890(aspS_1)
CSCI : HDCHBGLK_01726(aspS2)
CHYL : CE91St63_27890(aspC_3)
CSH : Closa_3356 Closa_3667
ANR : Ana3638_11235(aspS) Ana3638_16400(aspS)
ACEL : acsn021_12000(aspC_1) acsn021_27120(aspC_3)
ACHT : bsdcttw_12320(aspC_1) bsdcttw_29040(aspC_2)
AHB : bsdtb5_12880(aspC_1) bsdtb5_19410(aspC_2)
MALA : NCTC10135_00561(lysS_2)
SSPB : CP982_00925(aspS) CP982_00940
MSAG : GCM10017556_08330(aspC)
VMA : VAB18032_27436(aspC)
ACTR : Asp14428_26790(aspC)
ASIC : Q0Z83_073590(aspS_1)
KBB : ccbrp13_45010(aspC_1)
DEIN : DAAJ005_12735(aspS)
SLR : L21SP2_3338 L21SP2_3488
MEHF : MmiHf6_09410(aspS2)
MEES : MmiEs2_13190(aspS2)
MJK : N2V74_00105(aspS) N2V74_05745(aspS)
HDL : HALDL1_05425(aspC) HALDL1_06470
HALA : Hrd1104_02075(aspS)
HACB : Hbl1158_03280(aspS)
HRU : Halru_0012 Halru_1156
TVO : TVG1147365(TVG1147365)
SACR : SacRon12I_03710(aspC)
NIR : NSED_04875 NSED_06225
NKR : NKOR_04905 NKOR_06405
NID : NPIRD3C_1051(aspS) NPIRD3C_1327(aspS)
NIN : NADRNF5_0866(aspS) NADRNF5_1182(aspS)
NIW : Nisw_00385(aspS) Nisw_08115(aspS)
NCL : C5F47_03150 C5F47_04405
NOX : C5F49_04315 C5F49_06080
NUE : C5F50_06455 C5F50_08080
NIP : NsoK4_02395(aspS) NsoK4_04315(aspS)
NZT : NZOSNM25_000811 NZOSNM25_001053
NCT : NMSP_0573(aspS_1) NMSP_0847(aspS_2)
NGA : Ngar_c02730(aspS1) Ngar_c18880(aspS2)
NVN : NVIE_003450(aspS1) NVIE_014140(aspS2)
TAA : NMY3_02651(asnS_1) NMY3_03112(asnS_2)
NFN : NFRAN_0257(aspS) NFRAN_0528(aspS)
NCV : NCAV_0746(aspS) NCAV_1231(aspS)
CSY : CENSYa_0241 CENSYa_0611
NBV : T478_0773(aspS) T478_0884(aspS)
TAH : SU86_000905 SU86_001760
NIU : DSQ19_05200 DSQ19_06215
NCK : QVH35_09265(aspS) QVH35_10440(aspS)
NDV : NDEV_1112(aspS) NDEV_1176(aspS)
CCAI : NAS2_0491 NAS2_1309
LOKI : Lokiarch_26910(aspS)
» show all
Taxonomy
Reference
Authors
Ibba M, Soll D.
Title
Aminoacyl-tRNA synthesis.
Journal
Reference
Authors
Schmitt E, Moulinier L, Fujiwara S, Imanaka T, Thierry JC, Moras D.
Title
Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: archaeon specificity and catalytic mechanism of adenylate formation.
Journal
Reference
Authors
Becker HD, Kern D.
Title
Thermus thermophilus: a link in evolution of the tRNA-dependent amino acid amidation pathways.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 6.1.1.23
ExPASy - ENZYME nomenclature database: 6.1.1.23
LinkDB
All DBs