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EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.7.3.4-999 - more comparisons of wild-type and mutant enzyme kinetics, overview 739402
Display the word mapDisplay the reaction diagram Show all sequences 2.7.3.4-999 - more steady-state kinetic analysis, overview. Analysis of quaternary structure and cooperativity in ligand-binding by ITC: absence of inter-subunit cooperativity in forming the PsTK–TSAC 738077
Display the word mapDisplay the reaction diagram Show all sequences 2.7.3.40.082 - Taurocyamine mutant enzyme K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C 721715
Display the word mapDisplay the reaction diagram Show all sequences 2.7.3.40.1 - N-taurocyamine pH 8.0, 25°C 642485
Display the word mapDisplay the reaction diagram Show all sequences 2.7.3.40.14 - Taurocyamine mutant enzyme T68A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C 721715
Display the word mapDisplay the reaction diagram Show all sequences 2.7.3.40.153 - Taurocyamine mutant enzyme K69A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C 721715
Display the word mapDisplay the reaction diagram Show all sequences 2.7.3.40.184 - Taurocyamine mutant enzyme H67A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C 721715
Display the word mapDisplay the reaction diagram Show all sequences 2.7.3.40.205 - Taurocyamine mutant enzyme K95A, in 100 mM Tris-HCl, at pH 8.0 and 25°C 721715
Display the word mapDisplay the reaction diagram Show all sequences 2.7.3.40.217 - Taurocyamine mutant enzyme K69R/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C 721715
Display the word mapDisplay the reaction diagram Show all sequences 2.7.3.40.269 - Taurocyamine isoform PK1, in 100 mM Tris-HCl, at pH 8.0 and 25°C 722083
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