Glycerol catabolism in wild-type and mutant strains ofPseudomonas aeruginosa |
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Authors: | Sara M. McCowen Paul V. Phibbs Jr. Thomas W. Feary |
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Affiliation: | (1) Department of Biology, Virginia Commonwealth University, 816 Park Avenue, 23284 Richmond, Virginia, USA;(2) Department of Microbiology, Medical College of Virginia, Virginia Commonwealth University, 23298 Richmond, Virginia, USA;(3) Department of Microbiology, Louisiana State University, School of Dentistry, 70119 New Orleans, Louisiana, USA |
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Abstract: | Glycerol uptake, glycerol kinase (EC 2.7.1.30) and glycerol-3-phosphate dehydrogenase (EC 1.1.99.5) activities are specifically induced during growth ofPseudomonas aeruginosa PAO on either glycerol or glycerol-3-phosphate. Mutants of strain PAO unable to grow on both glycerol and glycerol-3-phosphate were isolated. Mutant PFB 121 was deficient in an inducible, membrane-bound, pyridine nucleotide-independent, glycerol-3-phosphate dehydrogenase activity and PFB 82 was deficient in glycerol uptake and glycerol kinase and glycerol-3-phosphate dehydrogenase activities. Each mutant spontaneously reverted to wild phenotype, which indicates that each contained a single genetic lesion. These results demonstrate that membrane-bound, inducible glycerol-3-phosphate dehydrogenase is required for catabolism of both glycerol and glycerol-3-phosphate and provide suggestive evidence for a single regulatory locus that controls the synthesis of glycerol uptake, glycerol kinase, and glycerol-3-phosphate dehydrogenase inP. aeruginosa. |
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