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Literature summary 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

EC Number Inhibitors Comment Organism Structure
6.1.1.6 3'-Deoxyadenosine 5'-triphosphate inhibitor in aminoacylation, good substrate in ATP-diphosphate exchange Saccharomyces cerevisiae

KM Value [mM]

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

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.6 Saccharomyces cerevisiae
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-
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Substrates and Products (Substrate)

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