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. 1975 Jun;148(3):505–511. doi: 10.1042/bj1480505

Tricarboxylic acid-cycle and related enzymes in restricted facultative methylotrophs.

J Colby, L J Zatman
PMCID: PMC1165569  PMID: 991

Abstract

The isolation is described of pure cultures of three non-methane-utilizing methylotrophic bacteria which, together with the previously described Bacillus PM6, have a very limited range of growth substrates; these organisms are designated "restricted facultative' methylotrophs. Two of these isolates, W6A and W3A1, grow only on glucose out of 50 non-C1 compounds tested, whereas the third isolate S2A1 and Bacillus PM6 grow on betaine, glucose, gluconate, alanine, glutamate, citrate and nutrient agar, but not on any of a further 56 non-C1 compounds. Crude sonic extracts of trimethylamine-grown and glucose-grown W6A and W3A1 isolates, and of trimethylamine-grown C2A1 (an obligate methylotroph) contain (i) no detectable 2-oxogltarate dehydrogenase activity, (ii) very low or zero specific activities of succinate dehydrogenase and succinyl-CoA synthetase and (iii) NAD+-dependent isocitrate dehydrogenase activity. Extracts of trimethylamine-grown PM6 and S2A1 methylotrophs have (i) very low 2-oxoglutarate dehydrogenase specific activities, (ii) comparatively high specific activities of succinate dehydrogenase, malate dehydrogenase and succinyl-CoA synthetase and (iii) NADP+-dependent isocitrate dehydrogenase activity but no NAD+-dependent isocitrate dehydrogenase activity. The activities of most of these enzymes are increased during growth on glucose, alanine, glutamate or citrate, but only very low 2-oxoglutarate dehydrogenase activities are present under all growth conditions. The restricted facultative methylotrophs grow on certain non-C1 compounds in the absence of 2-oxoglutarate dehydrogenase and, in some cases, of other enzymes of the tricarboxylic acid cycle; these lesions cannot therefore be the sole cause of obligate methylotrophy.

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Selected References

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

  1. Amarasingham C. R., Davis B. D. Regulation of alpha-ketoglutarate dehydrogenase formation in Escherichia coli. J Biol Chem. 1965 Sep;240(9):3664–3668. [PubMed] [Google Scholar]
  2. Anthony C., Zatman L. J. The microbial oxidation of methanol. 1. Isolation and properties of Pseudomonas sp. M27. Biochem J. 1964 Sep;92(3):609–614. doi: 10.1042/bj0920609. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Colby J., Zatman L. J. Enzymological aspects of the pathways for trimethylamine oxidation and C1 assimilation of obligate methylotrophs and restricted facultative methylotrophs. Biochem J. 1975 Jun;148(3):513–520. doi: 10.1042/bj1480513. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Colby J., Zatman L. J. Hexose phosphate synthese and tricarboxylic acid-cycle enzymes in bacterium 4B6, an obligate methylotroph. Biochem J. 1972 Aug;128(5):1373–1376. doi: 10.1042/bj1281373. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Colby J., Zatman L. J. Trimethylamine metabolism in obligate and facultative methylotrophs. Biochem J. 1973 Jan;132(1):101–112. doi: 10.1042/bj1320101. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Dahl J. S., Mehta R. J., Hoare D. S. New obligate methylotroph. J Bacteriol. 1972 Feb;109(2):916–921. doi: 10.1128/jb.109.2.916-921.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Davey J. F., Whittenbury R., Wilkinson J. F. The distribution in the methylobacteria of some key enzymes concerned with intermediary metabolism. Arch Mikrobiol. 1972;87(4):359–366. doi: 10.1007/BF00409135. [DOI] [PubMed] [Google Scholar]
  8. HIRSCH P., CONTI S. F. BIOLOGY OF BUDDING BACTERIA. II. GROWTH AND NUTRITION OF HYPHOMICROBIUM SPP. Arch Mikrobiol. 1964 Jun 26;48:358–367. doi: 10.1007/BF00405979. [DOI] [PubMed] [Google Scholar]
  9. Kelly D. P. Autotrophy: concepts of lithotrophic bacteria and their organic metabolism. Annu Rev Microbiol. 1971;25:177–210. doi: 10.1146/annurev.mi.25.100171.001141. [DOI] [PubMed] [Google Scholar]
  10. Kennedy S. I., Fewson C. A. Enzymes of the mandelate pathway in Bacterium N.C.I.B. 8250. Biochem J. 1968 Apr;107(4):497–506. doi: 10.1042/bj1070497. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. MUKHERJEE B. B., MATTHEWS J., HORNEY D. L., REED L. J. RESOLUTION AND RECONSTITUTION OF THE ESCHERICHIA COLI ALPHA-KETOGLUTARATE DEHYDROGENASE COMPLEX. J Biol Chem. 1965 May;240:2268–2269. [PubMed] [Google Scholar]
  12. PEEL D., QUAYLE J. R. Microbial growth on C1 compounds. I. Isolation and characterization of Pseudomonas AM 1. Biochem J. 1961 Dec;81:465–469. doi: 10.1042/bj0810465. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Smith A. J., London J., Stanier R. Y. Biochemical basis of obligate autotrophy in blue-green algae and thiobacilli. J Bacteriol. 1967 Oct;94(4):972–983. doi: 10.1128/jb.94.4.972-983.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. YOSHIDA A., FREESE E. ENZYMATIC PROPERTIES OF ALANINE DEHYDROGENASE OF BACILLUS SUBTILIS. Biochim Biophys Acta. 1965 Feb 22;96:248–262. [PubMed] [Google Scholar]

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