RT Journal Article SR Electronic(1) A1 Seno, E. T. A1 Chater, K. F.YR 1983 T1 Glycerol Catabolic Enzymes and Their Regulation in Wild-type and Mutant Strains of Streptomyces coelicolor A3(2) JF Microbiology, VO 129 IS 5 SP 1403 OP 1413 DO https://doi.org/10.1099/00221287-129-5-1403 PB Microbiology Society, SN 1465-2080, AB 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., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-129-5-1403