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. 1964 Oct;88(4):896–903. doi: 10.1128/jb.88.4.896-903.1964

LACTATE-DEGRADING SYSTEM IN BUTYRIBACTERIUM RETTGERI SUBJECT TO GLUCOSE REPRESSION

Charles L Wittenberger 1, Ann S Haaf 1
PMCID: PMC314830  PMID: 14219052

Abstract

Wittenberger, Charles L. (National Institute of Dental Research, U.S. Public Health Service, Bethesda, Md.), and Ann S. Haaf. Lactate-degrading system in Butyribacterium rettgeri subject to glucose repression. J. Bacteriol. 88:896–903. 1964.—The ability of Butyribacterium rettgeri to utilize lactate as the main energy source for growth requires the formation of a lactate-degrading system. The precise nature of this system is unknown, but preliminary evidence suggests that cellular acquisition of lactate-decomposing activity involves the formation of a nonpyridine nucleotide-linked lactic dehydrogenase. This enzyme, which can couple lactate oxidation to the reduction of ferricyanide [K3Fe(CN)6-lactic de-hydrogenase (LDH)], is absent from glucose-grown cells; this observation appears to account for the inability of such cells to decompose lactate even though they may form lactate from glucose. The formation of K3Fe(CN)6-LDH in growing cultures requires the addition of lipoic acid to the medium, and is repressed by glucose, pyruvate, or fructose. When any of the latter substrates are included in the growth medium with lactate, nicotinamide adenine dinucleotide-linked LDH activity is present in cells at markedly higher levels than it is in cells grown on lactate alone.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. KLINE L., BARKER H. A. A new growth factor required by Butyribacterium rettgeri. J Bacteriol. 1950 Sep;60(3):349–363. doi: 10.1128/jb.60.3.349-363.1950. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. KLINE L., PINE L., BARKER H. A. METABOLIC ROLE OF THE BR FACTOR IN BUTYRIBACTERIUM RETTGERI. J Bacteriol. 1963 May;85:967–975. doi: 10.1128/jb.85.5.967-975.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. KLINE L., PINE L., GUNSALUS I. C., BARKER H. A. Probable identity of the growth promoting factor for Butyribacterium rettgeri with other biologically-active substances. J Bacteriol. 1952 Oct;64(4):467–472. doi: 10.1128/jb.64.4.467-472.1952. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. MAGASANIK B. Catabolite repression. Cold Spring Harb Symp Quant Biol. 1961;26:249–256. doi: 10.1101/sqb.1961.026.01.031. [DOI] [PubMed] [Google Scholar]
  5. MAGASANIK B., NEIDHARDT F. C. The effect of glucose on the induced biosynthesis of bacterial enzymes in the presence and absence of inducing agents. Biochim Biophys Acta. 1956 Aug;21(2):324–334. doi: 10.1016/0006-3002(56)90016-6. [DOI] [PubMed] [Google Scholar]
  6. NEIDHARDT F. C., MAGASANIK B. Reversal of the glucose inhibition of histidase biosynthesis in Aerobacter aerogenes. J Bacteriol. 1957 Feb;73(2):253–259. doi: 10.1128/jb.73.2.253-259.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. PINE L., HAAS V., BARKER H. A. Metabolism of glucose by Butyribacterium rettgeri. J Bacteriol. 1954 Aug;68(2):227–230. doi: 10.1128/jb.68.2.227-230.1954. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. RICKENBERG H. V., LESTER G. The preferential synthesis of beta-galactosidase in Escherichia coli. J Gen Microbiol. 1955 Oct;13(2):279–284. doi: 10.1099/00221287-13-2-279. [DOI] [PubMed] [Google Scholar]

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