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Literature summary for 6.1.1.6 extracted from

  • Freist, W.; Cramer, F.
    Phenylalanyl-tRNA, lysyl-tRNA, isoleucyl-tRNA and arginyl-tRNA synthetases. Substrate specificity in the ATP-diphosphate exchange with regard to ATP analogs (1980), Eur. J. Biochem., 107, 47-50.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
3'-Deoxyadenosine 5'-triphosphate inhibitor in aminoacylation, good substrate in ATP-diphosphate exchange Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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additional information Km values of ATP analogues in ATP-diphosphate exchange Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + lysine + tRNALys
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Saccharomyces cerevisiae AMP + L-lysyl-tRNALys + diphosphate
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additional information lysine-dependent ATP-diphosphate exchange reaction: lysine + ATP + enzyme/lysine-AMP-enzyme + diphosphate Saccharomyces cerevisiae ?
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additional information substrate specificity in the ATP-diphosphate exchange with regard to ATP analogs Saccharomyces cerevisiae ?
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?