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Results 1 - 10 of 151 > >>
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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 1.1.1.357-999 - more AKR1C isozymes kinetics analysis, steady-state Michaelis-Menten kinetics 761761
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.357-999 - more Km-value for the 17beta-oxidation of testosterone is 0.00067 mM, and Km-value for the 17beta-reduction of androstenedione is 0.00138 mM 725345
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.357-999 - more steady-state kinetics 743736, 760734
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.357-999 - more steady-state kinetics and thermodynamics. The effects of temperature on kcat/Km for 3alpha-HSD/CR acting on androsterone, 2-decalol, and cyclohexanol show the reactions are entropically favorable but enthalpically unfavorable. Thermodynamic analysis from the temperature-dependent values of Km and kcat shows the binding of the E-NAD+ complex with either 2-decalol or cyclohexanol to form the ternary complex is endothermic and entropy-driven, and the subsequent conversion to the transition state is both enthalpically and entropically unfavorable 760867
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.357-999 - more steady-state kinetics of 3alpha-HSD/CR catalyzed reaction of NADþ with androsterone and the truncated analogues, overview. The uniform binding energy from the B-ring of steroids with the active site of 3alpha-HSD/CR equally contributes 2.1 kcal/mol to stabilize both the transition state and ground state of the ternary complex, leading to the similarity in kcat for 2-decalol and cyclohexanol. Differential binding interactions of the remote BCD-ring and CD-ring of androsterone with the active site of 3alpha-HSD/CR contribute 8.5 and 6.4 kcal/mol to the stabilization of the transition state, respectively. The removal of the carbonyl group at C17 of androsterone has small effects on catalysis. Both uniform and differential binding energies from the remote sites of androsterone compared to cyclohexanol contribute to the 3a-HSD/CR catalysis, resulting in the increases in kcat and kcat/KB 742260
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.357-999 - more steady-state kinetics, and stopped-flow study, kinetics of enzyme mutants P185A, P185G, T188A, and T188S showing an increase in kcat, Ka drosterone and KiNAD and equal primary isotope effects of DV and D(V/K) 743632
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.3570.00007 - NADPH in 100 mM potassium phosphate, pH 7.0, at 25°C 654626
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.3570.0001 - 5alpha-androstan-17-beta-ol-3-one mutant F217S, pH 7.4, 25°C 739957
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.3570.0002 - 5alpha-pregnan-20alpha-ol-3-one mutant F217S, pH 7.4, 25°C 739957
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.3570.0002 - NADP+ mutant F217S, pH 7.4, 25°C 739957
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