KEGG   ENZYME: 6.1.1.23Help
Entry
EC 6.1.1.23                 Enzyme                                 

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
ATP [CPD:C00002];
L-aspartate [CPD:C00049];
tRNAAsx
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
Aminoacyl-tRNA biosynthesis
Orthology
K09759  
nondiscriminating aspartyl-tRNA synthetase
Genes
BAN: 
BA_2186(aspC)
BAR: 
GBAA_2186(aspC)
BAT: 
BAS2031(aspC)
BAH: 
BAI: 
BAA_2247(aspC)
BAX: 
BANT: 
BANR: 
BAL: 
BCE: 
BC2169(aspC)
BCZ: 
BCZK1981(aspC)
BCR: 
BCB: 
BCU: 
BCG: 
BCQ: 
BCQ_2153(aspC)
BCX: 
BCA_2271(aspC)
BNC: 
BCF: 
BCER: 
BCK_23745(aspC)
BTK: 
BTL: 
BALH_1944(aspC)
BTB: 
BTT: 
BTC: 
BTF: 
BTM: 
BTG: 
BTB_c22300(aspS1)
BTI: 
BTG_09045(aspC)
BTN: 
BTHT: 
BTHU: 
BWE: 
BTY: 
CAC: 
CA_C2979(aspC) CA_C3564(aspC)
CAE: 
SMB_G3015(aspS) SMB_G3605(aspC)
CAY: 
CEA_G2986(aspC1) CEA_G3571(aspC3)
CPF: 
CPF_0770(aspC)
CBO: 
CBO1019(aspC)
CBA: 
CLB_1059(aspC)
CBH: 
CLC_1072(aspC)
CBY: 
CLM_1174(aspC)
CBL: 
CLK_0462(aspC)
CBK: 
CLL_A2506(aspC)
CBB: 
CLD_3547(aspC)
CBI: 
CLJ_B1064(aspC)
CBF: 
CLI_1101(aspC)
CBM: 
CBJ: 
CBE: 
Cbei_2126(aspC)
CCB: 
CSR: 
Cspa_c31980(aspS2) Cspa_c35300(aspS3)
CPAS: 
AMT: 
Amet_3390(aspC)
EHA: 
RUM: 
CLE: 
RHO: 
RIX: 
RIM: 
ROB: 
RTO: 
CPY: 
CSH: 
CST: 
ERE: 
ERT: 
ERA: 
BPRS: 
NBR: 
ROP: 
SCT: 
SCY: 
BCV: 
ICA: 
NCA: 
KFL: 
SRO: 
FRE: 
AMD: 
AMED_1332(aspC)
AMN: 
RAM_06755(aspC)
AMM: 
AMES_1324(aspC)
AMZ: 
B737_1325(aspC)
AOI: 
AORI_6069(aspC)
MAU: 
MIL: 
VMA: 
AMS: 
ASE: 
ACPL_1611(aspC)
ACTN: 
L083_1857(aspC)
AFS: 
AFR_09230(aspC)
CAI: 
SNA: 
PUV: 
PUV_24770(aspS-A)
TAZ: 
TREAZ_1118(aspS_2)
TPI: 
SCD: 
SSM: 
STA: 
STQ: 
SFC: 
SLR: 
DRA: 
DR_1055(aspC)
DGE: 
Dgeo_0796(aspC)
DDR: 
DMR: 
DPT: 
DGO: 
DPD: 
TRA: 
TTH: 
TTC1087(aspC)
TTJ: 
TTHA1452(aspC)
TTS: 
TTL: 
TSC: 
TSC_c18940(aspS2)
THC: 
TOS: 
MRB: 
MRE: 
MSV: 
OPR: 
MHD: 
SBE: 
 » show all
Taxonomy
Reference
1  [PMID:10966471]
  Authors
Ibba M, Soll D.
  Title
Aminoacyl-tRNA synthesis.
  Journal
Annu. Rev. Biochem. 69 (2000) 617-50.
  Organism
Escherichia coli
Reference
2  [PMID:9724658]
  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
EMBO. J. 17 (1998) 5227-37.
  Organism
Pyrococcus kodakaraensis
Reference
3  [PMID:9789000]
  Authors
Becker HD, Kern D.
  Title
Thermus thermophilus: a link in evolution of the tRNA-dependent amino acid amidation pathways.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 12832-7.
  Organism
Thermus thermophilus
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9027-32-1

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