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Literature summary for 6.1.1.20 extracted from

  • Khvorova, A.M.; Motorin, Y.A.; Wolfson, A.D.
    Crucial role of pyrophosphate in the aminoacylation of E. coli tRNAPhe by yeast phenylalanyl-tRNA synthetase (1992), FEBS Lett., 311, 139-142.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
E. coli tRNAPhe inhibition by formation of a tight complex of the enzyme with the diphosphate formed during the aminoacylation Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00017
-
tRNAPhe substrate from yeast Saccharomyces cerevisiae
0.0032
-
tRNAPhe substrate from E. coli Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-phenylalanine + tRNAPhe
-
Saccharomyces cerevisiae AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
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