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BRENDA support

Literature summary for 6.1.1.2 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]

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

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
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Source Tissue

Source Tissue Comment Organism Textmining
pancreas
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Bos taurus
-

Substrates and Products (Substrate)

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