Literature summary extracted from

Jackson, C.J.; Lamb, D.C.; Marczylo, T.H.; Warrilow, A.G.; Manning, N.J.; Lowe, D.J.; Kelly, D.E.; Kelly, S.L.
A novel sterol 14alpha-demethylase/ferredoxin fusion protein (MCCYP51FX) from Methylococcus capsulatus represents a new class of the cytochrome P450 superfamily (2002), J. Biol. Chem., 277, 46959-46965.

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
1.14.15.36	Iron	3.9 molecules per enzyme molecule, 3Fe-4S center of ferredoxin component, one iron molecule bound to heme	Methylococcus capsulatus

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
1.14.15.36	62000	-	x * 62000, SDS-PAGE, recombinant enzyme	Methylococcus capsulatus
1.14.15.36	706000	-	gel filtration	Methylococcus capsulatus

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.14.15.36	Methylococcus capsulatus	-	natural fusion protein of enzyme and ferredoxin	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.14.15.36	lanosterol + [reduced NADPH-hemoprotein reductase] + O2	activity depends on presence of natural fusion protein ferredoxin	Methylococcus capsulatus	? + formate + [oxidized NADPH-hemoprotein reductase] + H2O	-	?

Subunits

EC Number	Subunits	Comment	Organism
1.14.15.36	dodecamer	x * 62000, SDS-PAGE, recombinant enzyme	Methylococcus capsulatus

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Release 2023.1 (January 2023)