Biology:Steroid 15beta-monooxygenase
From HandWiki
| 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] 15beta-hydroxyprogesterone + oxidized ferredoxin + H2O
The enzyme from Bacillus megaterium hydroxylates a variety of 3-oxo-Delta4-steroids in position 15beta.
References
- ↑ "Purification and characterization of cytochrome P-450meg". The Journal of Biological Chemistry 254 (12): 5264–71. June 1979. doi:10.1016/S0021-9258(18)50589-5. PMID 109432.
- ↑ "Characterization of a cytochrome P-450-dependent steroid hydroxylase system present in Bacillus megaterium". The Journal of Biological Chemistry 251 (9): 2831–8. May 1976. doi:10.1016/S0021-9258(17)33564-0. PMID 177422.
- ↑ "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. June 2004. doi:10.1016/j.bbrc.2004.05.037. PMID 15178459.
- ↑ "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. November 2009. doi:10.1016/j.bbapap.2009.07.012. PMID 19635596.
- ↑ "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. June 2008. doi:10.1002/cbic.200700670. PMID 18481342.
External links
- Steroid+15beta-monooxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)
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