Steroid 15beta-monooxygenase

Steroid 15beta-monooxygenase
Identifiers
EC number 1.14.15.8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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

  1. Berg, A.; Ingelman-Sundberg, M.; Gustafsson, J.A. (1979). "Purification and characterization of cytochrome P-450meg". J. Biol. Chem. 254 (12): 5264–5271. PMID 109432.
  2. Berg, A.; Gustafsson, J.A.; 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.
  3. Lisurek, M.; Kang, M.J.; Hartmann, R.W.; 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.
  4. Goni, G.; Zollner, A.; Lisurek, M.; Velazquez-Campoy, A.; Pinto, S.; Gomez-Moreno, C.; Hannemann, F.; Bernhardt, R.; 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.
  5. Lisurek, M.; Simgen, B.; Antes, I.; 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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