EC 1.14.14.154 - Sterol 14α-demethylase

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IntEnz Enzyme Nomenclature
EC 1.14.14.154

Names

Accepted name:
sterol 14α-demethylase
Other names:
lanosterol 14-demethylase
lanosterol 14α-demethylase
obtusufoliol 14-demethylase
sterol 14-demethylase
cytochrome P450 51
CYP51
ERG11
Systematic name:
sterol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (14-methyl cleaving)

Reactions

Cofactor

Comments:

This cytochrome P450 (heme-thiolate) enzyme acts on a range of steroids with a 14α-methyl group, such as obtusifoliol and lanosterol. The enzyme catalyses a hydroxylation and a reduction of the 14α-methyl group, followed by a second hydroxylation, resulting in the elimination of formate and formation of a 14(15) double bond. Formerly EC 1.14.13.70.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00081
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (35) [show] [UniProt]

References

  1. Bak, S., Kahn, R.A., Olsen, C.E. and Halkier, B.A.
    Cloning and expression in Escherichia coli of the obtusifoliol 14α-demethylase of Sorghum bicolor (L.) Moench, a cytochrome P450 orthologous to the sterol 14α-demethylases (CYP51) from fungi and mammals.
    Plant J. 11 : 191-201 (1997). [PMID: 9076987]
  2. Aoyama, Y. and Yoshida, Y.
    Different substrate specificities of lanosterol 14α-demethylase (P450-14DM) of Saccharomyces cerevisiae and rat liver of 24-methylene-24,25-dihydrolanosterol and 24,25-dihydrolanosterol.
    Biochem. Biophys. Res. Commun. 178 : 1064-1071 (1991). [PMID: 1872829]
  3. Aoyama, Y. and Yoshida, Y.
    The 4β-methyl group of substrate does not affect the activity of lanosterol 14α-demethylase (P45014DM) of yeast: differences between the substrate recognition by yeast and plant sterol 14α-demethylases.
    Biochem. Biophys. Res. Commun. 183 : 1266-1272 (1992). [PMID: 1567403]
  4. Alexander, K., Akhtar, M., Boar, R.B., McGhie, J.F. and Barton, D.H.R.
    The removal of the 32-carbon atom as formic acid in cholesterol biosynthesis.
    J. Chem. Soc. Chem. Commun. 383-385 (1972).
  5. Aoyama, Y., Yoshida, Y., Sato, R.
    Yeast cytochrome P-450 catalyzing lanosterol 14 alpha-demethylation. II. Lanosterol metabolism by purified P-450(14)DM and by intact microsomes.
    J. Biol. Chem. 259 : 1661-1666 (1984). [PMID: 6420412]
  6. Yoshida, Y., Aoyama, Y.
    Yeast cytochrome P-450 catalyzing lanosterol 14 alpha-demethylation. I. Purification and spectral properties.
    J. Biol. Chem. 259 : 1655-1660 (1984). [PMID: 6363414]

[EC 1.14.14.154 created 2001 as EC 1.14.13.70, modified 2013, transferred 2018 EC 1.14.14.154]