Binding of reduced and oxidized nicotinamide adenine dinucleotide to pig heart supernatant malate dehydrogenase

Biochemistry ◽  
1979 ◽  
Vol 18 (16) ◽  
pp. 3611-3616 ◽  
Author(s):  
Robert E. Johnson ◽  
John A. Rupley
Keyword(s):  
Malate Dehydrogenase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine

Oxidation−Reduction Properties of the Regulatory Disulfides of Sorghum Chloroplast Nicotinamide Adenine Dinucleotide Phosphate−Malate Dehydrogenase†

Biochemistry ◽  
2000 ◽  
Vol 39 (12) ◽  
pp. 3344-3350 ◽  
Author(s):  
Masakazu Hirasawa ◽  
Eric Ruelland ◽  
Isabelle Schepens ◽  
Emmanuelle Issakidis-Bourguet ◽  
Myroslawa Miginiac-Maslow ◽  
...  
Keyword(s):  
Malate Dehydrogenase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Nicotinamide Adenine ◽  
Oxidation Reduction

scholarly journals The stereospecificity of nicotinamide–adenine dinucleotide-dependent oxidoreductases from plants

1972 ◽  
Vol 127 (2) ◽  
pp. 335-343 ◽  
Author(s):  
D. D. Davies ◽  
A. Teixeira ◽  
P. Kenworthy
Keyword(s):  
Malate Dehydrogenase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine ◽  
Plant Enzymes ◽  
Metabolic Sequence

1. The stereospecificity of 20 enzymes from plants is reported. 2. The stereospecificity of all known forms of malate dehydrogenase in plants and animals has been shown to be A-specific. 3. The generalization that ‘the stereospecificity of a particular reaction is independent of the source of the enzyme’ is confirmed for a total of 12 plant enzymes. 4. A new generalization is proposed: ‘When a metabolic sequence involves consecutive nicotinamide–adenine dinucleotide-dependent reactions, the dehydrogenases have the same stereospecificity.’

scholarly journals The stereospecificity of sequential nicotinamide-adenine dinucleotide-dependent oxidoreductases in relation to the evolution of metabolic sequences

1975 ◽  
Vol 149 (3) ◽  
pp. 553-557 ◽  
Author(s):  
K H do Nascimento ◽  
D D Davies
Keyword(s):  
Pseudomonas Putida ◽  
Malate Dehydrogenase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine ◽  
Hydroxypyruvate Reductase ◽  
Metabolic Sequence ◽  
The Common

The generalization that ‘when a metabolic sequence involves consecutive nicotinamide-adenine dinucleotide-dependent reactions, the dehydrogenases have the same stereospecificity’ was tested and confirmed for three metabolic sequences. (1) NAD+-xylitol (D-xylulose) dehydrogenase and NADP+-xylitol (L-xylulose) dehydrogenase are both B-specific. (2) D-Mannitol 1-phosphate dehydrogenase and D-sorbitol 6-phosphate dehydrogenase are both B-specific. (3) meso Tartrate dehydrogenase and oxaloglycollate reductive decarboxylase are both A-specific. Other dehydrogenases associated with the metabolism of meso-tartrate in Pseudomonas putida, such as hydroxypyruvate reductase and tartronate semialdehyde reductase, were also shown to be A-specific. Malate dehydrogenase from Pseudomonas putida was A-specific, and the proposition is discussed that the common A-stereospecificity among the dehydrogenases involved in meso-tartrate metabolism reflects their origin from malate dehydrogenase.

scholarly journals The role of nicotinamide–adenine dinucleotide phosphate-dependent malate dehydrogenase and isocitrate dehydrogenase in the supply of reduced nicotinamide–adenine dinucleotide phosphate for steroidogenesis in the superovulated rat ovary

1970 ◽  
Vol 117 (1) ◽  
pp. 73-83 ◽  
Author(s):  
A. P. F. Flint ◽  
R. M. Denton
Keyword(s):  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Nicotinamide Adenine ◽  
Tissue Homogenate ◽  
Kinetic Properties ◽  
Rat Ovary ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Effect Of Glucose

1. Superovulated rat ovary was found to contain high activities of NADP–malate dehydrogenase and NADP–isocitrate dehydrogenase. The activity of each enzyme was approximately four times that of glucose 6-phosphate dehydrogenase and equalled or exceeded the activities reported to be present in other mammalian tissues. Fractionation of a whole tissue homogenate of superovulated rat ovary indicated that both enzymes were exclusively cytoplasmic. The tissue was also found to contain pyruvate carboxylase (exclusively mitochondrial), NAD–malate dehydrogenase and aspartate aminotransferase (both mitochondrial and cytoplasmic) and ATP–citrate lyase (exclusively cytoplasmic). 2. The kinetic properties of glucose 6-phosphate dehydrogenase, NADP–malate dehydrogenase and NADP–isocitrate dehydrogenase were determined and compared with the whole-tissue concentrations of their substrates and NADPH; NADPH is a competitive inhibitor of all three enzymes. The concentrations of glucose 6-phosphate, malate and isocitrate in incubated tissue slices were raised at least tenfold by the addition of glucose to the incubation medium, from the values below to values above the respective Km values of the dehydrogenases. Glucose doubled the tissue concentration of NADPH. 3. Steroidogenesis from acetate is stimulated by glucose in slices of superovulated rat ovary incubated in vitro. It was found that this stimulatory effect of glucose can be mimicked by malate, isocitrate, lactate and pyruvate. 4. It is concluded that NADP–malate dehydrogenase or NADP–isocitrate dehydrogenase or both may play an important role in the formation of NADPH in the superovulated rat ovary. It is suggested that the stimulatory effect of glucose on steroidogenesis from acetate results from an increased rate of NADPH formation through one or both dehydrogenases, brought about by the increases in the concentrations of malate, isocitrate or both. Possible pathways involving the two enzymes are discussed.

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