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Results 1 - 6 of 6
EC Number Cofactor Commentary Reference
Show all pathways known for 1.1.1.245Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.245NAD+ - 12556, 246371, 286378, 667621
Show all pathways known for 1.1.1.245Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.245NAD+ isoenzyme II 286383
Show all pathways known for 1.1.1.245Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.245NAD+ temperature-induced conformational change is associated with the flexible loops directly involved in the substrate and coenzyme binding 667621
Show all pathways known for 1.1.1.245Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.245NADH enzyme exhibits linearity of NAD(H) binding at pH 9.8 and at moderate ionic strength, in addition to positive cooperativity at pH 7.8 and 6.8, and at pH 9.8 in the presence of salt. NADH binding is positively cooperative below 20°C and negatively cooperative at 40–50°. Steady-state kinetic measurements show that SsADH displays standard Michaelis–Menten kinetics between 35°C and 45°C, but exhibits positive and negative cooperativity for NADH oxidation below and above this range of temperatures, respectively. Mutant N249Y displays non-cooperative behavious in coenzyme binding under the same experimental conditions used for the wild-type enzyme 667502
Show all pathways known for 1.1.1.245Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.245NADP+ less than 5% activity than with NAD+ 12556
Show all pathways known for 1.1.1.245Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.245NADP+ weaker activity than with NAD+ 286378
Results 1 - 6 of 6