crystal structure of cholesterol oxidase from b.sterolicum
Identifiers
Symbol
Chol_subst-bind
Pfam
PF09129
Pfam clan
CL0277
InterPro
IPR015213
SCOP2
1i19 / SCOPe / SUPFAM
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
In enzymology, a cholesterol oxidase (EC 1.1.3.6) is an enzyme that catalyzes the chemical reaction
cholesterol + O2 cholest-4-en-3-one + H2O2
Thus, the two substrates of this enzyme are cholesterol and O2, whereas its two products are cholest-4-en-3-one and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is cholesterol:oxygen oxidoreductase. Other names in common use include cholesterol- O2 oxidoreductase, 3beta-hydroxy steroid oxidoreductase, and 3beta-hydroxysteroid:oxygen oxidoreductase. This enzyme participates in bile acid biosynthesis.
The substrate-binding domain found in some bacterial cholesterol oxidases is composed of an eight-stranded mixed beta-pleated sheet and six alpha-helices. This domain is positioned over the isoalloxazine ring system of the FAD cofactor bound by the FAD-binding domain and forms the roof of the active site cavity, allowing for catalysis of oxidation and isomerisation of cholesterol to cholest-4-en-3-one.[1]
^Coulombe R, Yue KQ, Ghisla S, Vrielink A (August 2001). "Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pair". J. Biol. Chem. 276 (32): 30435–41. doi:10.1074/jbc.M104103200. PMID 11397813.
and 22 Related for: Cholesterol oxidase information
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Ghoshroy, KB (21 Apr 1998). "Assessment of the role of an omega loop of cholesteroloxidase: a truncated loop mutant has altered substrate specificity". Biochemistry...
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