3-Acetylpyridine hypoxanthine dinucleotide is an analogue of nicotinamide adenine dinucleotide (NAD) which may be used in mechanistic studies of NAD-dependent enzymes and enzymes that act upon NAD itself.
Archives of biochemistry and biophysics, 284(2), 285-291 (1991-02-01)
Initial velocity, product inhibition, and substrate inhibition studies suggest that the endogenous lactate dehydrogenase activity of duck epsilon-crystallin follows an order Bi-Bi sequential mechanism. In the forward reaction (pyruvate reduction), substrate inhibition by pyruvate was uncompetitive with inhibition constant of
The Biochemical journal, 245(2), 407-414 (1987-07-15)
The structural requirements of the NADP+ molecule as a coenzyme in the oxidative decarboxylation reaction catalysed by pigeon liver malic enzyme were studied by kinetic and fluorimetric analyses with various NADP+ analogues and fragments. The substrate L-malate had little effect
Biochimica et biophysica acta, 994(2), 172-179 (1989-02-02)
Rat liver S-adenosylhomocysteinase, a homotetramer, was resolved by treatment with acid ammonium sulfate into apoenzyme and NAD. The apoenzyme thus prepared retained a tetrameric structure but differed in the mobility on nondenaturing polyacrylamide gel electrophoresis. The inactive apoenzyme was reactivated
Poly(ADP-ribosyl) transferase (pADPRT) catalyzes the transfer of the ADP-ribose moiety from NAD+ onto proteins as well as onto protein-bound ADP-ribose. As a result, protein-bound polymers of ADP-ribose are formed. pADPRT itself contains several acceptor sites for ADP-ribose polymers and may
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