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Results 1 - 8 of 8
EC Number Cofactor Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.92(R)-NADPD deuterated cofactor derivative, the overall rate of catalysis is largely determined by the rate of hydride transfer upon replacement of NADPH by (R)-NADPD as the coenzyme, overview 685231
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.92FAD - 657625, 659371, 710979, 726716, 763827, 763862, 764116, 764264, 764409, 765535
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.92FAD binding structure involving Arg337, overview 671189
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.92FAD residue R337, which is conserved in other Baeyer-Villiger monooxygenases, is positioned close to the flavin cofactor 685231
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.92NADH poor activity with NADH, kinetics, binding mode, overview 710979
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.92NADPH - 659371, 671189, 671682, 675467, 677171, 678885, 684245, 685231, 690110, 726716, 726793, 727379, 728163, 728164, 744548, 745991, 763827, 763862, 764116, 764264, 764409, 765535
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.92NADPH can not be replaced by NADH 657625
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.92NADPH PAMO is a type I Baeyer-Villiger monooxygenase, that strongly prefers NADPH over NADH as an electron donor, the function of NADPH in catalysis cannot be easily replaced by NADH. The conserved R217 is essential for binding the adenine moiety of the nicotinamide coenzyme while it also contributes to the recognition of the 2'-phosphate moiety of NADPH, binding mode, overview. T218 and K336 do not have a strong effect on the coenzyme specificity 710979
Results 1 - 8 of 8