Role of adenine ring and adenine ribose of nicotinamide adenine dinucleotide in binding and catalysis with alcohol, lactate, and glyceraldehyde-3-phosphate dehydrogenases.
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Covalent binding of 3-pyridinealdehyde nicotinamide adenine dinucleotide and substrate to glyceraldehyde 3-phosphate dehydrogenase.
Glyceraldehyde 3-phosphate dehydrogenase (D-glyceraldehyde-3-phoshate:nicotinamide adenine dinucleotide oxidoreductase (phosphorylating), EC 1.2.1.12) forms a complex with 3-pyridinealdehyde-NAD which survives precipitation with 7% perchloric acid. The molar ratio bound 3-pyridinealdehyde-NAD to the enzyme is 2.5 to 2.9. Lactate, malate, and alcohol dehydrogenases do not form acid-precipitable ...
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Saccharomyces cerevisiae contains two distinct l-glutamate dehydrogenases. These enzymes are affected in a reciprocal fashion by growth on ammonia or dicarboxylic amino acids as the nitrogen source. The specific activity of the nicotinamide adenine dinucleotide phosphate (NADP) (anabolic) enzyme is highest in ammonia-grown cells and is reduced in cells grown on glutamate or aspartate. Conversel...
متن کاملMeasurement of nicotinamide adenine dinucleotide & nicotinamide adenine dinucleotide phosphate in tomato leaves.
As part of an investigation of the growth of tomato plants supplied with either nitrate or ammonium nitrogen (6), leaves were assayed for NAD4 and NADP. Anderson and Vennesland (1) assayed NAD and NADP in various green tissues and reported recoveries between 50 % and 85 % of NAD and NADP added to spinach leaf extracts. Very low levels of NAD and NADP were recorded for tomato leaf extracts. Thes...
متن کاملA role for nicotinamide adenine dinucleotide glycohydrolase in the control of glyceraldehyde-3-phosphate dehydrogenase activity.
Tumor nicotinamide adenine dinudeotide (NAD) glycohydrolase (EC.3.2.2.5) was purified 500-fold, and this preparation was used to study the influence of NAD glycohydrolase on the NAD + content and activity of crystalline glyceraldehyde-3phosphate dehydrogenase. The pseudomonomolecular velocity constant, k, for the hydrolysis of free NAD + was 5-fold that of the constant for the enzyme-bound NAD ...
متن کاملInhibition of rat liver nicotinamide adenine dinucleotide kinase by reduced nicotinamide adenine dinucleotide phosphate.
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, ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1977
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)40242-0