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Literature summary for 6.1.1.12 extracted from

  • Choi, H.; Gabriel, K.; Schneider, J.; Otten, S.; McClain, W.H.
    Recognition of acceptor-stem structure of tRNA(Asp) by Escherichia coli aspartyl-tRNA synthetase (2003), RNA, 9, 386-393.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-aspartate + tRNAAsp Escherichia coli protein-RNA recognition between the enzyme and tRNA is highly specific and essential for cell viability AMP + diphosphate + L-aspartyl-tRNAAsp
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Reaction

Reaction Comment Organism Reaction ID
ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp protein-RNA recognition mechanism, backbone interactions are an important functional component of the tRNA synthetase interaction Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate + tRNAAsp wild-type Escherichia coli tRNAAsp and some recombinant acceptor stem mutants from Saccharomyces cerevisiae, overview Escherichia coli AMP + diphosphate + L-aspartyl-tRNAAsp
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?
ATP + L-aspartate + tRNAAsp protein-RNA recognition between the enzyme and tRNA is highly specific and essential for cell viability Escherichia coli AMP + diphosphate + L-aspartyl-tRNAAsp
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?
additional information no activity with wild-type tRNAAsp and several acceptor stem mutants from Saccharomyces cerevisiae, overview Escherichia coli ?
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?

Synonyms

Synonyms Comment Organism
Aspartic acid translase
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Escherichia coli
Aspartyl ribonucleate synthetase
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Escherichia coli
aspartyl ribonuleic synthetase
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Escherichia coli
Aspartyl-transfer ribonucleic acid synthetase
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Escherichia coli
Aspartyl-transfer RNA synthetase
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Escherichia coli
Aspartyl-tRNA synthetase
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Escherichia coli