J Bacteriol 103(1): 144-152
Regulation of Proline Degradation in <em>Salmonella typhimurium</em>
Abstract
The pathway for proline degradation in Salmonella typhimurium appears to be identical to that found in Escherichia coli and Bacillus subtilis. Δ-Pyrroline-5-carboxylic acid (P5C) is an intermediate in the pathway; its formation consumes molecular oxygen. Assays were devised for proline oxidase and the nicotinamide adenine dinucleotide phosphate-specific P5C dehydrogenase activities. Both proline-degrading enzymes, proline oxidase and P5C dehydrogenase, are induced by proline and are subject to catabolite repression. Three types of mutants were isolated in which both enzymes are affected: constitutive mutants, mutants with reduced levels of enzyme activity, and mutants unable to produce either enzyme. Most of the mutants isolated for their lack of P5C dehydrogenase activity have a reduced level of proline oxidase activity. All the mutations are cotransducible. A genetic map of some of the mutations is presented. The actual effector of the pathway appears to be proline.
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- BERTANI G. Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli. J Bacteriol. 1951 Sep;62(3):293–300.[PMC free article] [PubMed] [Google Scholar]
- Brill WJ, Magasanik B. Genetic and metabolic control of histidase and urocanase in Salmonella typhimurium, strain 15-59. J Biol Chem. 1969 Oct 10;244(19):5392–5402. [PubMed] [Google Scholar]
- Demerec M, Adelberg EA, Clark AJ, Hartman PE. A proposal for a uniform nomenclature in bacterial genetics. Genetics. 1966 Jul;54(1):61–76.[PMC free article] [PubMed] [Google Scholar]
- FRANK L, RANHAND B. PROLINE METABOLISM IN ESCHERICHIA COLI. 3. THE PROLINE CATABOLIC PATHWAY. Arch Biochem Biophys. 1964 Aug;107:325–331. [PubMed] [Google Scholar]
- Laishley EJ, Bernlohr RW. Regulation of arginine and proline catabolism in Bacillus licheniformis. J Bacteriol. 1968 Aug;96(2):322–329.[PMC free article] [PubMed] [Google Scholar]
- LOWRY OH, ROSEBROUGH NJ, FARR AL, RANDALL RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Meiss HK, Brill WJ, Magasanik B. Genetic control of histidine degradation in Salmonella typhimurium, strain LT-2. J Biol Chem. 1969 Oct 10;244(19):5382–5391. [PubMed] [Google Scholar]
- MUELLER-HILL B, RICKENBERG HV, WALLENFELS K. SPECIFICITY OF THE INDUCTION OF THE ENZYMES OF THE LAC OPERON IN ESCHERICHIA COLI. J Mol Biol. 1964 Nov;10:303–318. [PubMed] [Google Scholar]
- Sanderson KE. Revised linkage map of Salmonella typhimurium. Bacteriol Rev. 1967 Dec;31(4):354–372.[PMC free article] [PubMed] [Google Scholar]
- Scaife J, Beckwith JR. Mutational alteration of the maximal level of Lac operon expression. Cold Spring Harb Symp Quant Biol. 1966;31:403–408. [PubMed] [Google Scholar]
- Silverstone AE, Magasanik B, Reznikoff WS, Miller JH, Beckwith JR. Catabolite sensitive site of the lac operon. Nature. 1969 Mar 15;221(5185):1012–1014. [PubMed] [Google Scholar]
- STRECKER HJ. The interconversion of glutamic acid and proline. II. The preparation and properties of delta 1-pyrroline-5-carboxylic acid. J Biol Chem. 1960 Jul;235:2045–2050. [PubMed] [Google Scholar]
- STRECKER HJ. PURIFICATION AND PROPERTIES OF RAT LIVER ORNITHINE DELTA-TRANSAMINASE. J Biol Chem. 1965 Mar;240:1225–1230. [PubMed] [Google Scholar]
- WILLSON C, PERRIN D, COHN M, JACOB F, MONOD J. NON-INDUCIBLE MUTANTS OF THE REGULATOR GENE IN THE "LACTOSE" SYSTEM OF ESCHERICHIA COLI. J Mol Biol. 1964 Apr;8:582–592. [PubMed] [Google Scholar]