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
Steroid 15beta-monooxygenase
Identifiers
EC number1.14.15.8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

The enzyme from Bacillus megaterium hydroxylates a variety of 3-oxo-Delta4-steroids in position 15beta.

References

  1. Berg A, Ingelman-Sundberg M, Gustafsson JA (June 1979). "Purification and characterization of cytochrome P-450meg". The Journal of Biological Chemistry. 254 (12): 5264–71. PMID 109432.
  2. Berg A, Gustafsson JA, Ingelman-Sundberg M (May 1976). "Characterization of a cytochrome P-450-dependent steroid hydroxylase system present in Bacillus megaterium". The Journal of Biological Chemistry. 251 (9): 2831–8. PMID 177422.
  3. Lisurek M, Kang MJ, Hartmann RW, Bernhardt R (June 2004). "Identification of monohydroxy progesterones produced by CYP106A2 using comparative HPLC and electrospray ionisation collision-induced dissociation mass spectrometry". Biochemical and Biophysical Research Communications. 319 (2): 677–82. doi:10.1016/j.bbrc.2004.05.037. PMID 15178459.
  4. Goñi G, Zöllner A, Lisurek M, Velázquez-Campoy A, Pinto S, Gómez-Moreno C, Hannemann F, Bernhardt R, Medina M (November 2009). "Cyanobacterial electron carrier proteins as electron donors to CYP106A2 from Bacillus megaterium ATCC 13368". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1794 (11): 1635–42. doi:10.1016/j.bbapap.2009.07.012. PMID 19635596.
  5. Lisurek M, Simgen B, Antes I, Bernhardt R (June 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): 1439–49. doi:10.1002/cbic.200700670. PMID 18481342.
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