1887

Abstract

SUMMARY: Glycerol: NADP 2-oxidoreductase (EC 1.1.1.156) was isolated from , purified and characterized. It had an of 57000, and SDS-PAGE revealed two polypeptides, of 25000 and 30000. Its coenzyme requirement was satisfied exclusively by NADP. The pH optimum for glycerol oxidation was 9.5, for dihydroxyacetone reduction 6.0. Rates of oxidation with some structurally related diols were three- to six-fold lower than for glycerol, while glyceraldehyde and other carbonyl compounds showed negligible rates of reduction. Neither monovalent nor divalent cations activated the enzyme. Apparent and values were determined. The enzyme is similar to glycerol dehydrogenases isolated from and from but differs considerably from the glycerol: NAD 2-oxidoreductase of .

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/content/journal/micro/10.1099/00221287-135-3-697
1989-03-01
2019-11-14
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-135-3-697
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