A novel type of pyridine nucleotide-disulfide oxidoreductase is essential for NAD+- and NADPH-dependent degradation of epoxyalkanes by Xanthobacter strain Py2
| Autor: | A.H. Westphal, J. Swaving, A. de Kok, J.A.M. de Bont |
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| Rok vydání: | 1996 |
| Předmět: |
Mutant
Molecular Sequence Data Epoxide Microbiology Cofactor chemistry.chemical_compound Oxidoreductase Adenine nucleotide Alkanes NADH NADPH Oxidoreductases Amino Acid Sequence Sulfhydryl Compounds Xanthobacter Molecular Biology Dihydrolipoamide Dehydrogenase chemistry.chemical_classification Dihydrolipoamide dehydrogenase biology Gram-Negative Aerobic Bacteria Sequence Homology Amino Acid Adenine Nucleotides NAD chemistry Biochemistry biology.protein Epoxy Compounds NAD+ kinase Oxidoreductases NADP Research Article |
| Zdroj: | Journal of bacteriology. 178(22) |
| ISSN: | 0021-9193 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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