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Literature summary extracted from

  • Favorova, O.O.; Kochkina, L.L.; Meldrajs, J.A.; Kisselev, L.L.; Zinoviev, V.V.; Knorre, D.G.; Lavrik, O.I.; Malygin, E.G.; Nevinski, G.A.
    Kinetic parameters of tryptophan:tRNA ligase catalyzed ATP-[32P] pyrophosphate exchange as an approach to estimation of the order of substrate binding (1975), FEBS Lett., 56, 322-326.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.2 additional information
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additional information kinetic parameters of tryptophan-dependent ATP-diphosphate exchange reaction Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.2 Bos taurus
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-
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.1.1.2 pancreas
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Bos taurus
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.2 ATP + L-tryptophan + tRNATrp
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Bos taurus AMP + diphosphate + L-tryptophan-tRNATrp
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6.1.1.2 additional information tryptophan-dependent ATP-diphosphate exchange: tryptophan + ATP + enzyme /Trp-AMP-enzyme + diphosphate Bos taurus ?
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?