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Literature DB >> 8932325

A novel type of pyridine nucleotide-disulfide oxidoreductase is essential for NAD+- and NADPH-dependent degradation of epoxyalkanes by Xanthobacter strain Py2.

J Swaving¹, J A de Bont, A Westphal, A de Kok.

Abstract

Epoxide degradation in cell extracts of Xanthobacter strain Py2 has been reported to be dependent on NAD+ and dithiols. This multicomponent system has now been fractionated. A key protein encoded by a DNA fragment complementing a Xanthobacter strain Py2 mutant unable to degrade epoxides was purified and analyzed. This NADP-dependent protein, a novel type of pyridine nucleotide-disulfide oxidoreductase, is essential for epoxide degradation. NADPH, acting as the physiological cofactor, replaced the dithiols in epoxide conversion.

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Year: 1996 PMID： 8932325 PMCID： PMC178555 DOI： 10.1128/jb.178.22.6644-6646.1996

Source DB: PubMed Journal: J Bacteriol ISSN： 0021-9193 Impact factor: 3.490

17 in total

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Authors: J Swaving; C A Weijers; A J van Ooyen; J A de Bont
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Authors: S A Ensign
Journal: Appl Environ Microbiol Date: 1996-01 Impact factor: 4.792

9. Lipoamide dehydrogenase from Azotobacter vinelandii. Molecular cloning, organization and sequence analysis of the gene.

Authors: A H Westphal; A de Kok
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10. Cometabolic degradation of chlorinated alkenes by alkene monooxygenase in a propylene-grown Xanthobacter strain.

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7 in total

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