Glycerol Catabolic Enzymes and Their Regulation in Wild-type and Mutant Strains of Streptomyces coelicolor A3(2)
| Autor: | K. F. Chater, E. T. Seno |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
Glycerol
Arabinose chemistry.chemical_classification Glycerol-3-Phosphate Dehydrogenase (NAD+) Glycerol kinase biology Streptomyces coelicolor Wild type Glycerolphosphate Dehydrogenase Dehydrogenase biology.organism_classification Microbiology Streptomyces chemistry.chemical_compound Glucose Enzyme Gene Expression Regulation chemistry Biochemistry Enzyme Induction Glycerol Kinase Mutation Kinase activity |
| Zdroj: | Microbiology. 129:1403-1413 |
| ISSN: | 1465-2080 1350-0872 |
| Popis: | Summary: Assay procedures were developed for a soluble glycerol kinase [apparent K m (glycerol) 9 μm] and a probably membrane-associated, NAD-independent L-glycerol-3-phosphate dehydrogenase [apparent K m (L-glycerol 3-phosphate) 7 mM] present in Streptomyces coelicolor A3(2). Both enzymes were cold sensitive. They were co-ordinately induced (about 35-fold) by addition of glycerol to cultures growing on arabinose as sole carbon source. Induction was rifampicin sensitive. The dehydrogenase was absent from glycerol-sensitive mutants, and both kinase and dehydrogenase were absent from glycerol non-utilizing (but glycerol-resistant) mutants, demonstrating that the two enzymes are part of the major pathway of glycerol catabolism in S. coelicolor. Circumstantial evidence suggested that their inducer is glycerol 3-phosphate rather than glycerol. The enzymes were subject to co-ordinate repression by various carbon sources, of which glucose exerted the strongest effect (a fivefold repression). Previously described mutants resistant to 2-deoxyglucose, shown here to have very low glucose kinase activity, were defective in glucose repression of the glycerol enzymes. |
| Databáze: | OpenAIRE |
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