NAD+
-
347796,
390320,
390323,
656817,
693389,
724462,
725656,
741853,
762634,
762884,
763641
NAD+
a series of ALDHs have been shown to bind NAD in a conformation that results in a pro-R-specific hydride transfer during catalysis. The hydride transfer in FALDH is clearly pro-R specific. Residue Glu331 interacts with the ribose-backbone of NAD and assists correct cofactor binding and orientation
NAD+
activity of Bt-Aldh is doubled in the presence of NAD+ than NADP+
NAD+
NAD+ is a much better electron acceptor than NADP+, FAD or flavin mononucleotide
NAD+
the enzyme does not use NADP+ as cofactor
NAD+
the enzyme has a much greater specificity for NAD+ as cofactor than NADP+
NADP+
very high specificity and affinity, the residue Arg-210 contributes to the high cofactor affinity through a pi stacking interaction with the adenine ring system of the cofactor
NADPH
about 50% of the activity with NADH
