The stereospecificity of sequential nicotinamide-adenine dinucleotide-dependent oxidoreductases in relation to the evolution of metabolic sequences.
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.
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D001665:Binding Sites; D005075:Biological Evolution; D008353:Mannitol / Q000378:metabolism; D010088:Oxidoreductases / Q000378:metabolism; D013012:Sorbitol / Q000378:metabolism; D013644:Tartrates / Q000378:metabolism; D014993:Xylitol / Q000378:metabolism
D013644:Tartrates; D008353:Mannitol; D013012:Sorbitol; D010088:Oxidoreductases; D000429:Alcohol Oxidoreductases; D014993:Xylitol