Abstract
Regardless of the respiratory conditions of the culture, Escherichia coli synthesizes an active propanediol oxidoreductase. Under anaerobic conditions, the enzyme remained fully active and accomplished its physiological role, while under aerobic conditions, it was inactivated in a process that did not depend on protein synthesis or on the presence of a carbon source.
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Selected References
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- Boronat A., Aguilar J. Metabolism of L-fucose and L-rhamnose in Escherichia coli: differences in induction of propanediol oxidoreductase. J Bacteriol. 1981 Jul;147(1):181–185. doi: 10.1128/jb.147.1.181-185.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Boronat A., Aguilar J. Rhamnose-induced propanediol oxidoreductase in Escherichia coli: purification, properties, and comparison with the fucose-induced enzyme. J Bacteriol. 1979 Nov;140(2):320–326. doi: 10.1128/jb.140.2.320-326.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Boronat A., Caballero E., Aguilar J. Experimental evolution of a metabolic pathway for ethylene glycol utilization by Escherichia coli. J Bacteriol. 1983 Jan;153(1):134–139. doi: 10.1128/jb.153.1.134-139.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brawn K., Fridovich I. DNA strand scission by enzymically generated oxygen radicals. Arch Biochem Biophys. 1981 Feb;206(2):414–419. doi: 10.1016/0003-9861(81)90108-9. [DOI] [PubMed] [Google Scholar]
- Chen Y. M., Lin E. C. Post-transcriptional control of L-1,2-propanediol oxidoreductase in the L-fucose pathway of Escherichia coli K-12. J Bacteriol. 1984 Jan;157(1):341–344. doi: 10.1128/jb.157.1.341-344.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Chen Y. M., Lin E. C., Ros J., Aguilar J. Use of operon fusions to examine the regulation of the L-1,2-propanediol oxidoreductase gene of the fucose system in Escherichia coli K12. J Gen Microbiol. 1983 Nov;129(11):3355–3362. doi: 10.1099/00221287-129-11-3355. [DOI] [PubMed] [Google Scholar]
- Fucci L., Oliver C. N., Coon M. J., Stadtman E. R. Inactivation of key metabolic enzymes by mixed-function oxidation reactions: possible implication in protein turnover and ageing. Proc Natl Acad Sci U S A. 1983 Mar;80(6):1521–1525. doi: 10.1073/pnas.80.6.1521. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Johnson E. A., Levine R. L., Lin E. C. Inactivation of glycerol dehydrogenase of Klebsiella pneumoniae and the role of divalent cations. J Bacteriol. 1985 Oct;164(1):479–483. doi: 10.1128/jb.164.1.479-483.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Levine R. L. Oxidative modification of glutamine synthetase. II. Characterization of the ascorbate model system. J Biol Chem. 1983 Oct 10;258(19):11828–11833. [PubMed] [Google Scholar]
- Lin E. C. Glycerol dissimilation and its regulation in bacteria. Annu Rev Microbiol. 1976;30:535–578. doi: 10.1146/annurev.mi.30.100176.002535. [DOI] [PubMed] [Google Scholar]
- Ruch F. E., Jr, Lin E. C., Kowit J. D., Tang C. T., Goldberg A. L. In vivo inactivation of glycerol dehydrogenase in Klebsiella aerogenes: properties of active and inactivated proteins. J Bacteriol. 1980 Mar;141(3):1077–1085. doi: 10.1128/jb.141.3.1077-1085.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]