6.1.1.22: asparagine-tRNA ligase
This is an abbreviated version!
For detailed information about asparagine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.22
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6.1.1.22
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aminoacyl-trna
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asnrs
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aspartyl-trna
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malayi
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brugia
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aminoacylation
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amidotransferase
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asparaginylation
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asp-trnaasn
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glutaminyl-trna
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gatcabs
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filariasis
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transamidation
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nondiscriminating
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glu-trnagln
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mischarged
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misacylated
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asn-trna
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nd-asprs
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ammonia-dependent
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anti-ks
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lysyl-trna
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trnaasp
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histidyl-trna
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medicine
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drug development
- 6.1.1.22
- aminoacyl-trna
- asnrs
- aspartyl-trna
- malayi
- brugia
- aminoacylation
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amidotransferase
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asparaginylation
- asp-trnaasn
- glutaminyl-trna
- gatcabs
- filariasis
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transamidation
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nondiscriminating
- glu-trnagln
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mischarged
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misacylated
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asn-trna
- nd-asprs
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ammonia-dependent
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anti-ks
- lysyl-trna
- trnaasp
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histidyl-trna
- medicine
- drug development
Reaction
Synonyms
AS-AR, AsnRS, Asparagine synthetase A, Asparagine translase, asparagine tRNA synthetase, Asparagine--tRNA ligase, Asparaginyl transfer ribonucleic acid synthetase, Asparaginyl transfer RNA synthetase, asparaginyl tRNA synthetase, Asparaginyl-transfer ribonucleate synthetase, asparaginyl-transfer RNA synthetase, Asparaginyl-tRNA synthetase, Asparagyl-transfer RNA synthetase, class IIb asparaginyl-tRNA synthetase, More, NARS, NARS2, NRS, Potentially protective 63 kDa antigen, PYRAB02460, Synthetase, asparaginyl-transfer ribonucleate
ECTree
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Substrates Products
Substrates Products on EC 6.1.1.22 - asparagine-tRNA ligase
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REACTION DIAGRAM
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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with the aminoacylation step E + AA + ATP = E(AA-AMP) + diphosphate, and the amidation step E(AA-AMP) + tRNA = E+AA-tRNA + AMP
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r
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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AsnRS structure analysis shows binding of Mg2+-ATP in one active site and L-Asp-beta-NOH adenylate and Mg2+-diphosphate in the other active site. Active-site ordering and rearrangement during activation, overview. The AsnRSBm N-terminal extension binds tRNA, structure, overview
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
tRNAs from calf liver or Saccharomyces cerevisiae
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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with the aminoacylation step E + AA + ATP = E(AA-AMP) + diphosphate, and the amidation step E(AA-AMP) + tRNA = E+AA-tRNA + AMP
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r
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
Staphylococcus aureus FPR3757
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
substrate specificity
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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calculations of substrate binding and reaction mechanism, overview
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
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the high level of asparaginyl-tRNA synthetase expression reflects unusual metabolic demands associated with larval maturation
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additional information
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the parasite Brugia malayi enzyme, in analogy to the human enzyme, induces human leukocyte chemotaxis and activates G-protein-coupled receptors CXCR1 and CXCR2, but not CXCR3, filarial asparaginyl-tRNA synthetase, AsnRS, is known to be an immunodominant antigen that induces strong human immunoglobulin G3 responses and contributes to the development of chronic inflammatory disease such as lymphatic filariasis, overview
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additional information
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active site and ligand binding structure and mechanism, overview
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additional information
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human cytoplasmic aminoacyl-tRNA synthetases, which are autoantigens in idiopathic inflammatory myopathies, activate chemokine receptors on T lymphocytes, monocytes, and immature dendritic cells by recruiting immune cells that could induce innate and adaptive immune responses
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additional information
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active site and ligand binding structure and mechanism, overview
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additional information
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the enzyme is responsible for catalyzing the specific aminoacylation of tRNAAsn with asparagine, structural basis of the water-assisted asparagine recognition by the enzyme, two water molecules play a key role in the strict recognition of asparagine and the discrimination against aspartic acid by the AsnRS, overview, binding of Asn-AMP induces a conformational change in AsnRS
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additional information
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the enzyme is responsible for catalyzing the specific aminoacylation of tRNAAsn with asparagine, structural basis of the water-assisted asparagine recognition by the enzyme, two water molecules play a key role in the strict recognition of asparagine and the discrimination against aspartic acid by the AsnRS, overview, binding of Asn-AMP induces a conformational change in AsnRS
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additional information
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analysis of the molecular mechanism by molecular dynamics simulations and computational calculations using wild-type andmutant enzymes, overview
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additional information
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acylate Phaseolus aureus tRNA with an efficiency of 68% compared to the Phaseolus aureus enzyme. The tRNA of Vicia faba and Vicia sativa appears to be completely interchangeable
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additional information
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acylate Phaseolus aureus tRNA with an efficiency of 68% compared to the Phaseolus aureus enzyme. The tRNA of Vicia faba and Vicia sativa appears to be completely interchangeable
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additional information
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acylates tRNA of Vicia faba or Vicia sativa with an efficiency of 83% compared to Phaseolus aureus tRNA
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additional information
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isoasparagine (with 96% of the efficiency compared to L-Asn), aspartate-3-hydroxamate (with 81% of the efficiency compared to L-Asn) and 3-cyanoalanine (with 36% of the efficiency compared to L-Asn)
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