Polyol dehydrogenases. 1. The specificity of rat-liver polyol dehydrogenase
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چکیده
منابع مشابه
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...
متن کاملPolyol dehydrogenase of the silkworm.
Richert, D. A. & Westerfeld, W. W. (1957). Fed. Proc. 16, 238. Romanoff, E. B. & Hunt, C. A. (1954). Amer. J. Physiol. 179, 15. Schneider, W. C. & Hogeboom, G. H. (1952). J. biol. Chem. 195, 161. Sonnenschein, N. & Kopac, M. J. (1955). J. cell. comp. Ph.iol. 45, 361. Stevens, B. M. & Reid, E. (1956). Biochem. J. 64, 735. Umbreit, W. W. & Tonhazy, N. E. (1951a). J. biol. Chem. 191, 257. Umbreit,...
متن کاملGlycerol dehydrogenase. structure, specificity, and mechanism of a family III polyol dehydrogenase.
BACKGROUND Bacillus stearothermophilus glycerol dehydrogenase (GlyDH) (glycerol:NAD(+) 2-oxidoreductase, EC 1.1.1.6) catalyzes the oxidation of glycerol to dihydroxyacetone (1,3-dihydroxypropanone) with concomitant reduction of NAD(+) to NADH. Analysis of the sequence of this enzyme indicates that it is a member of the so-called iron-containing alcohol dehydrogenase family. Despite this sequenc...
متن کاملPolyol specificity of recombinant Arabidopsis thaliana sorbitol dehydrogenase studied by enzyme kinetics and in silico modeling
Polyols are enzymatically-produced plant compounds which can act as compatible solutes during periods of abiotic stress. Nicotinamide adenine dinucleotide(+)-dependent SORBITOL DEHYDROGENASE (SDH, E. C. 1.1.1.14) from Arabidopsis thaliana L. sorbitol dehydrogenase (AtSDH) is capable of oxidizing several polyols including sorbitol, ribitol, and xylitol. In the present study, enzymatic assays usi...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1954
ISSN: 0306-3283
DOI: 10.1042/bj0570518