Steroid 15beta-monooxygenase
Steroid 15beta-monooxygenase (EC 1.14.15.8, cytochrome P-450meg, cytochrome P450meg, steroid 15beta-hydroxylase, CYP106A2, BmCYP106A2) is an enzyme with systematic name progesterone,reduced-ferredoxin:oxygen oxidoreductase (15beta-hydroxylating) .[1][2][3][4][5] This enzyme catalyses the following chemical reaction
- progesterone + reduced ferredoxin + O2
15beta-hydroxyprogesterone + oxidized ferredoxin + H2O
The enzyme from Bacillus megaterium hydroxylates a variety of 3-oxo-Delta4-steroids in position 15beta.
References
- ↑ Berg, A., Ingelman-Sundberg, M. and Gustafsson, J.A. (1979). "Purification and characterization of cytochrome P-450meg". J. Biol. Chem. 254 (12): 5264–5271. PMID 109432.
- ↑ Berg, A., Gustafsson, J.A. and Ingelman-Sundberg, M. (1976). "Characterization of a cytochrome P-450-dependent steroid hydroxylase system present in Bacillus megaterium". J. Biol. Chem. 251 (9): 2831–2838. PMID 177422.
- ↑ Lisurek, M., Kang, M.J., Hartmann, R.W. and Bernhardt, R. (2004). "Identification of monohydroxy progesterones produced by CYP106A2 using comparative HPLC and electrospray ionisation collision-induced dissociation mass spectrometry". Biochem. Biophys. Res. Commun. 319 (2): 677–682. doi:10.1016/j.bbrc.2004.05.037. PMID 15178459.
- ↑ Goni, G., Zollner, A., Lisurek, M., Velazquez-Campoy, A., Pinto, S., Gomez-Moreno, C., Hannemann, F., Bernhardt, R. and Medina, M. (2009). "Cyanobacterial electron carrier proteins as electron donors to CYP106A2 from Bacillus megaterium ATCC 13368". Biochim. Biophys. Acta 1794 (11): 1635–1642. doi:10.1016/j.bbapap.2009.07.012. PMID 19635596.
- ↑ Lisurek, M., Simgen, B., Antes, I. and Bernhardt, R. (2008). "Theoretical and experimental evaluation of a CYP106A2 low homology model and production of mutants with changed activity and selectivity of hydroxylation". Chembiochem 9 (9): 1439–1449. doi:10.1002/cbic.200700670. PMID 18481342.
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