POLYOL DEHYDROGENASES OF AZOTOBACTER AGILIS

Polyol Dehydrogenases of Gluconobacter Oxydans.

The secondary hydroxyl group involved in the oxidation, and the cis-vicinal secondary hydroxyl group, must have a D configuration jvith respect to t,he primary alcohol group adjacent to the site of oxidation. This specific mode of otida,tion facilitated the synthesis of several new ketoses. In a series of papers, Hudson and Richtmyer and their a.ssociates described the microbiological synthesis...

Induced biochemical mutants to Azotobacter agilis.

Polyol dehydrogenases. 3. Galactitol dehydrogenase and D-iditol dehydrogenase.

Metabolic Studies of Azotobacter Agilis by the Use of a Mutant Deficient in Pyruvic Oxidase*

An account has been given elsewhere of the successful isolation of physiological x-ray mutants of Azotobacter agilis with genetic blocks in the substrate oxidation mechanisms (1). The present paper deals in greater detail with a mutant strain, designated A13, that was isolated as a variant unable to grow on glucose, and gives the methods used to characterize the particular deficiency responsibl...

Mannitol oxidase and polyol dehydrogenases in the digestive gland of gastropods: Correlations with phylogeny and diet

Mannitol oxidase and polyol dehydrogenases are enzymes that convert polyalcohols into sugars. Mannitol oxidase was previously investigated in terrestrial snails and slugs, being also present in a few aquatic gastropods. However, the overall distribution of this enzyme in the Gastropoda was not known. Polyol dehydrogenases are also poorly studied in gastropods and other mollusks. In this study, ...