Abstract
In Klebsiella aerogenes W70, there is an inducible pathway for the catabolism of ribitol consisting of at least two enzymes, ribitol dehydrogenase (RDH) and d-ribulokinase (DRK). These two enzymes are coordinately controlled and induced in response to d-ribulose, an intermediate of the pathway. Whereas wild-type K. aerogenes W70 are unable to utilize xylitol as a carbon and energy source, mutants constitutive for the ribitol pathway are able to utilize RDH to oxidize the unusual pentitol, xylitol, to d-xylulose. These mutants are able to grow on xylitol, presumably by utilization of the d-xylulose produced. Mutants constitutive for l-fucose isomerase can utilize the isomerase to convert d-arabinose to d-ribulose. In the presence of d-ribulose, RDH and DRK are induced, and such mutants are thus able to phosphorylate the d-ribulose by using the DRK of the ribitol pathway. Derivatives of an l-fucose isomerase-constitutive mutant were plated on d-arabinose, ribitol, and xylitol to select and identify mutations in the ribitol pathway. Using the transducing phage PW52, we were able to demonstrate genetic linkage of the loci involved. Three-point crosses, using constitutive mutants as donors and RDH−, DRK− double mutants as recipients and selecting for DRK+ transductants on d-arabinose, resulted in DRK+RDH+-constitutive, DRK+RDH+-inducible, and DRK+RDH−-inducible transductants but no detectable DRK+RDH− constitutive transductants, data consistent with the order rbtC-rbtD-rbtK, where rbtC is a control site and rbtD and rbtK correspond to the sites for the sites for the enzymes RDH and DRK, respectively.
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Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- ANDERSON R. L., WOOD W. A. Purification and properties of L-xylulokinase. J Biol Chem. 1962 Apr;237:1029–1033. [PubMed] [Google Scholar]
- Bisson T. M., Oliver E. J., Mortlock R. P. Regulation of pentitol metabolism by aerobacter aerogenes. II. Induction of the ribitol pathway. J Bacteriol. 1968 Mar;95(3):932–936. doi: 10.1128/jb.95.3.932-936.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
- COHEN S. Studies on D-ribulose and its enzymatic conversion to D-arabinose. J Biol Chem. 1953 Mar;201(1):71–84. [PubMed] [Google Scholar]
- Camyre K. P., Mortlock R. P. Growth of Aerobacter aerogenes on D-arabinose and L-xylose. J Bacteriol. 1965 Oct;90(4):1157–1158. doi: 10.1128/jb.90.4.1157-1158.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DISCHE Z., BORENFREUND E. A new spectrophotometric method for the detection and determination of keto sugars and trioses. J Biol Chem. 1951 Oct;192(2):583–587. [PubMed] [Google Scholar]
- LIN E. C., LERNER S. A., JORGENSEN S. E. A method for isolating constitutive mutants for carbohydrate-catabolizing enzymes. Biochim Biophys Acta. 1962 Jul 2;60:422–424. doi: 10.1016/0006-3002(62)90423-7. [DOI] [PubMed] [Google Scholar]
- LeBlanc D. J., Mortlock R. P. Metabolism of D-arabinose: a new pathway in Escherichia coli. J Bacteriol. 1971 Apr;106(1):90–96. doi: 10.1128/jb.106.1.90-96.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Leblanc D. J., Mortlock R. P. The metabolism of D-arabinose: alternate kinases for the phosphorylation of D-ribulose in Escherichia coli and Aerobacter aerogenes. Arch Biochem Biophys. 1972 Jun;150(2):774–781. doi: 10.1016/0003-9861(72)90097-5. [DOI] [PubMed] [Google Scholar]
- Lim R., Cohen S. S. D-phosphoarabinoisomerase and D-ribulokinase in Escherichia coli. J Biol Chem. 1966 Oct 10;241(19):4304–4315. [PubMed] [Google Scholar]
- MORTLOCK R. P., WOOD W. A. METABOLISM OF PENTOSES AND PENTITOLS BY AEROBACTER AEROGENES. I. DEMONSTRATION OF PENTOSE ISOMERASE, PENTULOKINASE, AND PENTITOL DEHYDROGENASE ENZYME FAMILIES. J Bacteriol. 1964 Oct;88:838–844. doi: 10.1128/jb.88.4.838-844.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MacPhee D. G., Sutherland I. W., Wilkinson J. F. Transduction in Klebsiella. Nature. 1969 Feb 1;221(5179):475–476. doi: 10.1038/221475a0. [DOI] [PubMed] [Google Scholar]
- Mortlock R. P., Fossitt D. D., Wood W. A. A basis for utlization of unnatural pentoses and pentitols by Aerobacter aerogenes. Proc Natl Acad Sci U S A. 1965 Aug;54(2):572–579. doi: 10.1073/pnas.54.2.572. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Oliver E. J., Bisson T. M., LeBlanc D. J., Mortlock R. P. D-Ribulose production by a mutant of Aerobacter aerogens. Anal Biochem. 1969 Feb;27(2):300–305. doi: 10.1016/0003-2697(69)90036-0. [DOI] [PubMed] [Google Scholar]
- Oliver E. J., Mortlock R. P. Growth of Aerobacter aerogenes on D-arabinose: origin of the enzyme activities. J Bacteriol. 1971 Oct;108(1):287–292. doi: 10.1128/jb.108.1.287-292.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Oliver E. J., Mortlock R. P. Metabolism of D-arabinose by Aerobacter aerogenes: purification of the isomerase. J Bacteriol. 1971 Oct;108(1):293–299. doi: 10.1128/jb.108.1.293-299.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- WOOD W. A., McDONOUGH M. J., JACOBS L. B. Rihitol and D-arabitol utilization by Aerobacter aerogenes. J Biol Chem. 1961 Aug;236:2190–2195. [PubMed] [Google Scholar]
- Wilson B. L., Mortlock R. P. Regulation of D-xylose and D-arabitol catabolism by Aerobacter aerogenes. J Bacteriol. 1973 Mar;113(3):1404–1411. doi: 10.1128/jb.113.3.1404-1411.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]