Literature DB >> 1633196

Characterization of aldehyde reductase of Sporobolomyces salmonicolor.

M Kataoka1, H Sakai, T Morikawa, M Katoh, T Miyoshi, S Shimizu, H Yamada.   

Abstract

An NADPH-dependent aldehyde reductase (EC 1.1.1.2) isolated from Sporobolomyces salmonicolor AKU 4429 was further characterized. The enzyme also catalyzed the reductions of D-glucuronate, D-glucose, D-xylose and D-galactose at high concentrations. Km values for D-glucuronate and D-glucose are 345 and 4270 mM, respectively. Quercetin, dicoumarol and some SH-reagents inhibited the enzyme activity. NH2-terminal amino acid sequence analysis showed that the S. salmonicolor enzyme is partially the same as the aldo-keto reductase family proteins in primary protein structure.

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Year:  1992        PMID： 1633196     DOI： 10.1016/0167-4838(92)90127-y

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  8 in total

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4.  Cloning of the aldehyde reductase gene from a red yeast, Sporobolomyces salmonicolor, and characterization of the gene and its product.

Authors:  K Kita; K Matsuzaki; T Hashimoto; H Yanase; N Kato; M C Chung; M Kataoka; S Shimizu
Journal:  Appl Environ Microbiol       Date:  1996-07       Impact factor: 4.792

5.  Cloning, overexpression, and mutagenesis of the Sporobolomyces salmonicolor AKU4429 gene encoding a new aldehyde reductase, which catalyzes the stereoselective reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (S)-4-chloro-3-hydroxybutanoate.

Authors:  K Kita; T Fukura; K I Nakase; K Okamoto; H Yanase; M Kataoka; S Shimizu
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8.  Purification and partial characterization of an aldo-keto reductase from Saccharomyces cerevisiae.

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  8 in total

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