ExplorEnz: EC 1.14.15.8

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1.14.15.8

Accepted name:

steroid 15β-monooxygenase

Reaction:

progesterone + 2 reduced [2Fe-2S] ferredoxin + O₂ = 15β-hydroxyprogesterone + 2 oxidized [2Fe-2S] ferredoxin + H₂O

Other name(s):

cytochrome P-450_meg; cytochrome P450_meg; steroid 15β-hydroxylase; CYP106A2; BmCYP106A2

Systematic name:

progesterone,reduced-ferredoxin:oxygen oxidoreductase (15β-hydroxylating)

Comments:

The enzyme from the bacterium Bacillus megaterium hydroxylates a variety of 3-oxo-Δ⁴-steroids in position 15β. Ring A-reduced, aromatic, and 3β-hydroxy-Δ⁴-steroids do not serve as substrates [2].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Berg, A., Ingelman-Sundberg, M. and Gustafsson, J.A. Purification and characterization of cytochrome P-450meg. J. Biol. Chem. 254 (1979) 5264–5271. [PMID: 109432]
2.	Berg, A., Gustafsson, J.A. and Ingelman-Sundberg, M. Characterization of a cytochrome P-450-dependent steroid hydroxylase system present in Bacillus megaterium. J. Biol. Chem. 251 (1976) 2831–2838. [PMID: 177422]
3.	Lisurek, M., Kang, M.J., Hartmann, R.W. and Bernhardt, R. Identification of monohydroxy progesterones produced by CYP106A2 using comparative HPLC and electrospray ionisation collision-induced dissociation mass spectrometry. Biochem. Biophys. Res. Commun. 319 (2004) 677–682. [DOI] [PMID: 15178459]
4.	Goni, G., Zollner, A., Lisurek, M., Velazquez-Campoy, A., Pinto, S., Gomez-Moreno, C., Hannemann, F., Bernhardt, R. and Medina, M. Cyanobacterial electron carrier proteins as electron donors to CYP106A2 from Bacillus megaterium ATCC 13368. Biochim. Biophys. Acta 1794 (2009) 1635–1642. [DOI] [PMID: 19635596]
5.	Lisurek, M., Simgen, B., Antes, I. and Bernhardt, R. Theoretical and experimental evaluation of a CYP106A2 low homology model and production of mutants with changed activity and selectivity of hydroxylation. ChemBioChem 9 (2008) 1439–1449. [DOI] [PMID: 18481342]

[EC 1.14.15.8 created 2010]