1887

Abstract

An inducible methanol dehydrogenase showing high activity with 2-chloroethanol was purified from 2-chloroethanol-grown cells of the 1, 2-dichloroethane utilizing bacterium GJ10. The enzyme consisted of a 60 kDa polypeptide that was associated with a 10 kDa polypeptide and contained pyrrolo-quinoline quinone (PQQ) as a prosthetic group. Chloroethanol-grown cells of strain GJ10 also contained an inducible NAD-dependent chloroacetaldehyde dehydrogenase. Its involvement in the metabolism of 2-chloroethanol was inferred from its absence in a 2-chloroethanol non-utilizing mutant. Three different isolates of that do not utilize 2-chloroethanol for growth produced chloroethanol dehydrogenase and chloroacetaldehyde dehydrogenase activities at similar levels as strain GJ10. It is concluded that both dehydrogenases are involved in the metabolism of natural compounds and due to their broad substrate specificity fortuitously also play a role in the metabolism of the xenobiotic compounds 1,2-dichloroethane and 2-chloroethanol.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-133-1-85
1987-01-01
2024-12-06
Loading full text...

Full text loading...

/deliver/fulltext/micro/133/1/mic-133-1-85.html?itemId=/content/journal/micro/10.1099/00221287-133-1-85&mimeType=html&fmt=ahah

References

  1. Alefounder P. R., Ferguson S. J. 1981; A periplasmic location for methanol dehydrogenase from Paracoccus denitrificans: implications for proton pumping by cytochrome aa3. Biochemical and Biophysical Research Communications 98:778–784
    [Google Scholar]
  2. Anthony C. 1982 The Biochemistry of Methylotrophs London: Academic Press;
    [Google Scholar]
  3. Anthony C., Zatman L. J. 1967; The microbial oxidation of methanol. Purification and properties of the alcohol dehydrogenase of Pseudomonas sp. M27. Biochemical Journal 104:953–959
    [Google Scholar]
  4. Beardsmore-Gray M., O’Keefe D. T., Anthony C. 1983; The methanol: cytochrome c oxidoreductase of methylotrophs. Journal of General Microbiology 129:923–933
    [Google Scholar]
  5. Duine J. A., Frank J. 1981a; Methanol dehydrogenase: a quinoprotein. In Microbial Growth in C1 Compounds pp. 31–41 Dalton H. Edited by London: Heyden;
    [Google Scholar]
  6. Duine J. A., Frank J. 1981b; Quinoprotein alcohol dehydrogenase from a non-methylotroph, Acinetobacter calcoaceticus. Journal of General Microbiology 122:201–209
    [Google Scholar]
  7. Janssen D. B., Scheper A., Without B. 1984; Biodegradation of 2-chloroethanol and 1,2-dichloro- ethane by pure bacterial cultures. In Innovations in Biotechnology pp. 169–178 Houwink E. H., Van der Meer R. R. Edited by Amsterdam: Elsevier;
    [Google Scholar]
  8. Janssen D. B., Scheper A., Dijkhuizen L., Witholt B. 1985; Degradation of halogenated aliphatic compounds by Xanthobacter autotrophicus GJ10. Applied and Environmental Microbiology 49:673–677
    [Google Scholar]
  9. Kasprzak A. A., Steenkamp D. J. 1983; Localization of the major dehydrogenases in two methylotrophs by radiochemical labeling. Journal of Bacteriology 156:348–353
    [Google Scholar]
  10. Keuning S., Janssen D. B., Witholt B. 1985; Purification and characterization of hydrolytic haloalkane dehalogenase from Xanthobacter autotrophicus GJ10. Journal of Bacteriology 163:635–639
    [Google Scholar]
  11. Laemmli U. K. 1970; Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature; London: 227680–685
    [Google Scholar]
  12. Patel R. N., Felix A. 1976; Microbial oxidation of methane and methanol: crystallization and properties of methanol dehydrogenase from Methylo- sinus sporium. Journal of Bacteriology 128:413–424
    [Google Scholar]
  13. Patel R. N., Hou C. T., Felix A. 1978; Microbial oxidation of methane and methanol: crystallization of methanol dehydrogenase and properties of holo- and apo-methanol dehydrogenase from Methylomonas methanica. Journal of Bacteriology 133:641–649
    [Google Scholar]
  14. Sahm H., Cox R. B., Quayle J. R. 1976; Metabolism of methanol by Rhodopseudomonas acidophila. Journal of General Microbiology 94:313–322
    [Google Scholar]
  15. Schär H. -P., Chemla P., Ghisalba O. 1985; Methanol dehydrogenase from Hyphomicrobium MS223. FEMS Microbiology Letters 26:117–122
    [Google Scholar]
  16. Sperl G. T., Forrest H. S., Gibson D. T. 1974; substrate specificity of the purified primary alcohol dehydrogenases from methanol-oxidizing bacteria. Journal of Bacteriology 18:541–550
    [Google Scholar]
  17. Stucki G., Krebser U., Leisinger T. 1983; Bacterial growth on 1,2-dichloroethane. Experientia 39:1271–1273
    [Google Scholar]
  18. Tunail N., Schlegel H. G. 1974; A new coryneform hydrogen bacterium: Corynebacterium autotrophicum strain 7C. I. Characterization of the wild type strain. Archives of Microbiology 100:341–350
    [Google Scholar]
  19. Weaver C. A., Lidstrom M. E. 1985; Methanol dissimilation in Xanthobacter H4-14: activities, induction and comparison to Pseudomonas AMI and Paracoccus denitrificans.. Journal of General Microbiology 131:2183–2197
    [Google Scholar]
  20. Wiegel J., Wilke D., Baumgarten J., Opitz R., Schlegel H. G. 1978; Transfer of the nitrogenfixing hydrogen bacterium Corynebacterium autotrophicum Baumgarten et al. to Xanthobacter gen. nov. International Journal of Systematic Bacteriology 28:573–581
    [Google Scholar]
  21. Wilke D., Schlegel H. G. 1979; A defective generalized transducing bacteriophage in Xanthobacter autotrophicus GZ29. Journal of General Microbiology 115:403–410
    [Google Scholar]
  22. Yamanaka K., Minoshima R. 1984; Comparison of two dye-linked alcohol dehydrogenases of Rhodopseudomonas acidophila: their substrate specificity and behavior toward oxygen. Agricultural and Biological Chemistry 48:171–179
    [Google Scholar]
/content/journal/micro/10.1099/00221287-133-1-85
Loading
/content/journal/micro/10.1099/00221287-133-1-85
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error