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Results 1 - 10 of 106 > >>
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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 1.5.1.40-999 - more analysis of the F420 redox moiety (FO)-dependent NADP+/NADPH redox process by stopped-flow spectrophotometry, steady state kinetics, overview 743386
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.40-999 - more steady-state kinetics 742904
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.40-999 - more substrate binding studies, steady-state and pre steady-state kinetic analysis with wild-type enzyme Fno and Ile135 Fno mutant variants, I135A, I135V, and I135G, overview. Steady-state kinetic analysis of wild-type Fno and the variants show classical Michaelis-Menten kinetics with varying FO concentrations. The data reveal a decreased kcat as side chain length decreased, with varying FO concentrations. The steady-state plots reveal non-Michaelis-Menten kinetic behavior when NADPH is varied. The double reciprocal plot of the varying NADPH concentrations displays a downward concave shape, while the NADPH binding curves gave Hill coefficients of less than 1. These data suggest that negative cooperativity occurs between the two identical monomers. The pre steady-state Abs420 versus time trace reveals biphasic kinetics, with a fast phase (hydride transfer) and a slow phase. The fast phase displays an increased rate constant as side chain length decreases. The rate constant for the second phase, remained about 2/s for each variant. Pre-steady-state data with F420 cofactor and NADPH for the enzyme Fno mutant variants reveal biphasic kinetics with a fast and slow phase, similar with wild-type Fno, overview 741811
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.40-999 - more the enzyme shows half-site reactivity and negative cooperativity (Koshland-Nemethy-Filmer model) in the reversible reduction of NADP+ through the transfer of a hydride from the reduced F420 cofactor, steady-state kinetic analysis revealing classical Michaelis-Menten kinetics with varying concentrations of the F420 redox moiety, and non-Michaelis-Menten kinetic behavior when NADPH is varied. Pre-steady-state, stopped flow, Single-turnover, and steady-state kinetics, detailed overview 741921
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.400.00027 - NADPH phase I, pH 6.5, 22°C, recombinant mutant I135A 741811
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.400.0007 - NADPH phase I, pH 6.5, 22°C, recombinant mutant I135V 741811
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.400.0023 - NADPH phase I, pH 6.5, 22°C, recombinant wild-type enzyme 741811
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.400.0028 - 1,5-dihydro-8-hydroxy-5-deazaflavin pH 7.0, 20°C 725326
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.400.0029 - NADPH phase II, pH 6.5, 22°C, recombinant mutant I135A 741811
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.400.0034 - coenzyme F420 pH 6.0, 22°C 711315
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