Literature DB >> 164267

The specificity of oxidase and kinase preparations from Pseudomonas fluorescens towards deoxyfluoromonosaccharides.

N F Taylor, L Hill, R Eisenthal.   

Abstract

With partially purified enzyme preparations from cell-free extracts of Pseudomonas fluorescens, 3-deoxy-3-fluoro-D-glucose and 3-deoxy-3-fluoro-D-gluconic acid are substrates for glucose oxidase (EC 1.1.3.4.) and gluconate dehydrogenase (EC 1.1.99.3), with K-m values 18.2 mM and 11.8 mM, respectively. The same enzymes that oxidize glucose and gluconic acid probably oxidize 3-deoxy-3-fluoro-D-glucose and 3-deoxy-3-fluoro-D-gluconic acid. The latter fluorinated carbohydrates and the presumed formation of 3-deoxy-3-fluoro-2-keto-D-gluconic acid, which has been isolated as a calcium salt and characterizied, are not substrates for gluconokinase (EC 2.7.1.12). Both 3-deoxy-3-fluoro-D-glucose and 3-deoxy-3-fluoro-D-gluconic acid act as competitive inhibitors of this enzyme preparation for gluconate, with K-i values 47.5 mM and 14.8 mM, respectively.

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Year:  1975        PMID: 164267     DOI: 10.1139/o75-009

Source DB:  PubMed          Journal:  Can J Biochem        ISSN: 0008-4018


  1 in total

1.  The active transport of 2-keto-D-gluconate in vesicles prepared from Pseudomonas purida.

Authors:  F Agbanyo; N F Taylor
Journal:  Biochem J       Date:  1985-05-15       Impact factor: 3.857

  1 in total

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