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Results 1 - 10 of 195 > >>
EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49-999 - more - 286819, 286982, 286984, 286986, 286987, 286988, 286991, 286992, 286996, 286998, 287001, 655712
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49-999 - more hyperbolic kinetics versus D-glucose 6-phosphate 722212
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49-999 - more kinetics 657147
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49-999 - more kinetics and thermodynamics, rapid equilibrium random bi bi kinetic model 655736
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49-999 - more kinetics, kinetic mechanism analysis, ternary-complex mechanism, overview 674379
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49-999 - more Michaelis-Menten kinetics 723340
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49-999 - more ping pong bi bi kinetic mechanism 673156
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49-999 - more steady-state kinetics of wild-type and mutant enzymes 672382, 673944
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49-999 - more the initial velocity plots of the enzyme follow the Michaelis-Menten equation in the absence of NADH. In its presence, however, the velocity versus substrate plots for NADP+ become sigmoidal but remain hyperbolic for glucose 6-phosphate as the variable substrate. Inhibition against both of the substrates of the enzyme by NADH is noncompetitive. The inhibition curves for NADH are also sigmoidal, suggesting a multisite binding of the inhibitor on the enzyme surface 722577
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49-999 - more thermodynamics, steady-state kinetics 657284
Results 1 - 10 of 195 > >>