Reversal by Nicotinamide Adenine Dinucleotide of the Inhibitory Action of Salicylate on Mitochondrial Malate Dehydrogenase

Nature ◽  
1964 ◽  
Vol 202 (4927) ◽  
pp. 96-97 ◽  
Author(s):  
M. J. H. SMITH ◽  
C. BRYANT ◽  
W. J. W. HINES
Keyword(s):  
Malate Dehydrogenase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Inhibitory Action ◽  
Nicotinamide Adenine ◽  
Mitochondrial Malate Dehydrogenase

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.

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