Purification and properties of polyol dehydrogenase from Cephalosporium chrysogenus.
A polyol dehydrogenase of broad specificity was purified 178-fold from extracts of the filamentous fungus Cephalosporium chrysogenum. The enzyme was found to act as an oxido-reductase in two substrate-coenzyme systems: D-sorbitol (or xylitol)-nicotinamide-adenine dinucleotide (NAD) and D-mannitol-nicotinamide adenine dinucleotide phosphate (NADP). The dehydrogenase was composed of five isozymes, which, as a mixture, exhibited these properties: Km to D-sorbitol and D-mannitol, 7.15 to 10(-2) M; PH optimum, 9 to 10; molecular weight, 300,000 subunit weight, 29,000; PI, 5.8 to 7.5. The NADP-linked activity was labile to treatment with heat or ethylenediaminetetraacetic acid. Mixed substrate assays support the hypothesis that both NAD-, and NADP-linked activities are associated with isozymes of a single dehydrogenase.
D000164:Acremonium / Q000201:enzymology*; D000429:Alcohol Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism; D050260:Carbohydrate Metabolism; D002474:Cell-Free System; D004492:Edetic Acid / Q000494:pharmacology; D005632:Fructose / Q000096:biosynthesis; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000302:isolation & purification; D008274:Magnesium / Q000494:pharmacology; D008353:Mannitol / Q000378:metabolism; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D013012:Sorbitol / Q000378:metabolism; D013237:Stereoisomerism
D007527:Isoenzymes; D009243:NAD; D005632:Fructose; D008353:Mannitol; D013012:Sorbitol; D009249:NADP; D004492:Edetic Acid; D000429:Alcohol Oxidoreductases; D008274:Magnesium