Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1981 Jun 15;196(3):781–786. doi: 10.1042/bj1960781

Studies on the substrate specificity and inducibility of cytochrome P-450meg.

A Berg, J J Rafter
PMCID: PMC1163098  PMID: 6797409

Abstract

The cytochrome P-450-dependent steroid 15 beta-hydroxylase system in Bacillus megaterium A.T.C.C. 13368 was investigated with regard to its appearance in the cell with respect to the growth curve of the organism, with regard to its inducibility by a number of agents (among them some of the classical inducers of the mammalian liver microsomal cytochrome P-450 system) and with regard to its capacity to convert non-steroidal substances into oxygenated compounds. The enzyme was found to reach a maximum concentration in the cell during the stationary phase of the growth curve. Of all the agents tested as inducers, none showed any capacity to induce cytochrome P-450meg. Finally, of the substances tested as substrates only aniline (p-hydroxylation) was metabolized by the microbial enzyme system. This conversion might be related to the general oxygenase activity of haemoproteins. It is concluded that the substrate specificity of the B. megaterium hydroxylase system is narrow.

Full text

PDF
782

Selected References

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

  1. Almé B., Bremmelgaard A., Sjövall J., Thomassen P. Analysis of metabolic profiles of bile acids in urine using a lipophilic anion exchanger and computerized gas-liquid chromatorgaphy-mass spectrometry. J Lipid Res. 1977 May;18(3):339–362. [PubMed] [Google Scholar]
  2. Berg A., Carlstrom K., Gustafsson J. A., Ingelman-Sundberg M. Demonstration of a cytochrome P-450-dependent steroid 15beta-hydroxylase in Bacillus megaterium. Biochem Biophys Res Commun. 1975 Oct 27;66(4):1414–1423. doi: 10.1016/0006-291x(75)90517-3. [DOI] [PubMed] [Google Scholar]
  3. Berg A., Gustafsson J. A., Ingelman-Sundberg M. Characterization of a cytochrome P-450-dependent steroid hydroxylase system present in Bacillus megaterium. J Biol Chem. 1976 May 10;251(9):2831–2838. [PubMed] [Google Scholar]
  4. Berg A., Ingelman-Sundberg M., Gustafsson J. A. Purification and characterization of cytochrome P-450meg. J Biol Chem. 1979 Jun 25;254(12):5264–5271. [PubMed] [Google Scholar]
  5. Broadbent D. A., Cartwright N. J. Bacterial attack on phenolic ethers. Resolution of a Nocardia O-demethylase and purification of a cytochrome P 450 component. Microbios. 1971 Jul;4(13):7–12. [PubMed] [Google Scholar]
  6. Dahlberg E., Snochowski M., Gustafsson J. A. Removal of hydrophobic compounds from biological fluids by a simple method. Anal Biochem. 1980 Aug;106(2):380–388. doi: 10.1016/0003-2697(80)90537-0. [DOI] [PubMed] [Google Scholar]
  7. Gustafsson J. A., Bergman J. Iodine- and chlorine-containing oxidation agents as hydroxylating catalysts in cytochrome P-450-dependent fatty acid hydroxylation reactions in rat liver microsomes. FEBS Lett. 1976 Nov;70(1):276–280. doi: 10.1016/0014-5793(76)80774-0. [DOI] [PubMed] [Google Scholar]
  8. Hare R. S., Fulco A. J. Carbon monoxide and hydroxymercuribenzoate sensitivity of a fatty acid (omega-2) hydroxylase from Bacillus megaterium. Biochem Biophys Res Commun. 1975 Jul 22;65(2):665–672. doi: 10.1016/s0006-291x(75)80198-7. [DOI] [PubMed] [Google Scholar]
  9. Hildebrandt A. G., Leibman K. C., Estabrook R. W. Metyrapone interaction with hepatic microsomal cytochrome P-450 from rats treated with phenobarbital. Biochem Biophys Res Commun. 1969 Oct 22;37(3):477–485. doi: 10.1016/0006-291x(69)90940-1. [DOI] [PubMed] [Google Scholar]
  10. Ho P. P., Fulco A. J. Involvement of a single hydroxylase species in the hydroxylation of palmitate at the omega-1, omega-2 and omega-3 positions by a preparation from Bacillus megaterium. Biochim Biophys Acta. 1976 May 27;431(2):249–256. doi: 10.1016/0005-2760(76)90145-4. [DOI] [PubMed] [Google Scholar]
  11. Matson R. S., Hare R. S., Fulco A. J. Characteristics of a cytochrome P-450-dependent fatty acid omega-2 hydroxylase from bacillus megaterium. Biochim Biophys Acta. 1977 Jun 22;487(3):487–494. doi: 10.1016/0005-2760(77)90218-1. [DOI] [PubMed] [Google Scholar]
  12. Mieyal J. J., Ackerman R. S., Blumer J. L., Freeman L. S. Characterization of Enzyme-like activity of human hemoglobin. Properties of the hemoglobin-P-450 reductase-coupled aniline hydroxylase system. J Biol Chem. 1976 Jun 10;251(11):3436–3441. [PubMed] [Google Scholar]
  13. Mieyal J. J., Blumer J. L. Accleration of autooxidation of human oxyhemoglobin by aniline and its relation to hemoglobin-catalyzed aniline hydroxylation. J Biol Chem. 1976 Jun 10;251(11):3442–3446. [PubMed] [Google Scholar]
  14. Miura Y., Fulco A. J. (Omega -2) hydroxylation of fatty acids by a soluble system from bacillus megaterium. J Biol Chem. 1974 Mar 25;249(6):1880–1888. [PubMed] [Google Scholar]
  15. NASH T. The colorimetric estimation of formaldehyde by means of the Hantzsch reaction. Biochem J. 1953 Oct;55(3):416–421. doi: 10.1042/bj0550416. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. OMURA T., SATO R. THE CARBON MONOXIDE-BINDING PIGMENT OF LIVER MICROSOMES. I. EVIDENCE FOR ITS HEMOPROTEIN NATURE. J Biol Chem. 1964 Jul;239:2370–2378. [PubMed] [Google Scholar]
  17. SAVAGE N. Preparation and properties of highly purified diaphorase. Biochem J. 1957 Sep;67(1):146–155. doi: 10.1042/bj0670146. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES