The Mechanism of Enzyme-catalyzed Reduced Nicotinamide Adenine Dinucleotide-dependent Reductions
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منابع مشابه
The mechanism of enzyme-catalyzed reduced nicotinamide adenine dinucleotide-dependent reductions. Substituent and isotope effects in the yeast alcohol dehydrogenase reaction.
Yeast alcohol dehydrogenase has been found to catalyze the reduction of a series of para-substituted benzaldehydes at markedly different rates. By steady state kinetic analysis, values of kB and ko have been obtained for yeast alcohol dehydrogenase reduction of $-Br-, p-Cl-, H-, &CH3, &CH80benzaldehyde by reduced nicotinamide adenine dinucleotide (NADH) and reduced nicotinamide adenine dinucleo...
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A reduced nicotinamide adenine dinucleotide (NADH)-dependent glutamate synthase has been detected and partially purified from crude extracts of Saccharomyces cerevisiae. The enzyme is specific for NADH, glutamine, and alpha-ketoglutarate (K(m) values of 2.6 muM, 1.0 mM, and 140 muM, respectively) and has a pH optimum between 7.1 and 7.7. The stoichiometry of the reaction has been determined as ...
متن کاملFormation of reduced nicotinamide adenine dinucleotide peroxide.
Incubation of NADH at neutral and slightly alkaline pH leads to the gradual absorption of 1 mol of H+. This uptake of acid requires oxygen and mainly yields anomerized NAD+ (NAD+), with only minimal formation od acid-modified NADH. The overall stoichiometry of the reaction is: NADH + H+ + 1/2O2 leads to H2O + NAD+, with NADH peroxide (HO2-NADH+) serving as the intermediate that anomerizes and b...
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Rat liver NAD kinase (ATP : NAD 2’-phosphotransferase, EC 2.7.1.23) was purified about 70-fold. The MichaelisMenten constants (Km) for NAD and ATP were 8 x 10e4 M and 2 x low3 M, respectively. NAD kinase activity was markedly inhibited by NADH and also NADPH. The Ki of NADH was approximately 1 X 10q4 M, and that of NADPH was approximately 5 X 10M5 M. Both inhibitions were competitive with NAD, ...
متن کاملProstaglandin metabolism. I. Cytoplasmic reduced nicotinamide adenine dinucleotide phosphate-dependent and microsomal reduced nicotinamide adenine dinucleotide-dependent prostaglandin E 9-ketoreductase activities in monkey and pigeon tissues.
Homogenates of pigeon heart, brain, lung, liver, and the formed elements of blood and of monkey brain, liver, spleen, kidney, lung, uterus, heart, and the formed elements of blood contain an enzyme which catalyzes the reduction of the 9-keto group of prostaglandin E to form prostaglandin F. The prostaglandin E 9-ketoreductase in all of these tissues uses NADPH much more effectively than NADH an...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1972
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(20)81798-0