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Literature summary for 1.1.3.6 extracted from

  • Kimberley Yue, Q.; Kass, I.J.; Sampson, N.S.; Vrielink, A.
    Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active site mutants (1999), Biochemistry, 38, 4277-4286.
    View publication on PubMed
Search for more literature for 1.1.3.6

Cloned(Commentary)

Cloned (Comment) Organism
-
 Streptomyces sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
vapor diffusion by hanging drop method, 1.5 A resolution, wild-type, E361Q, H447N and H447Q mutant, structure consists of FAD-binding and a steroid-binding domain with a large active site cavity in between Streptomyces sp.

Protein Variants

Protein Variants Comment Organism
E361Q H447Q mutant shows wild-type activity in isomerization, kcat for oxidation reaction is reduced 120fold, Km increases 2fold compared to wild-type, E361Q mutant has no isomerization activity, kcat is 30fold slower than for wild-type, Glu361 may therefore act as general base in oxidation reaction Streptomyces sp.
H447N H447Q mutant shows wild-type activity in isomerization, kcat for oxidation reaction is reduced 120fold, Km increases 2fold compared to wild-type, E361Q mutant has no isomerization activity, kcat is 30fold slower than for wild-type, Glu361 may therefore act as general base in oxidation reaction Streptomyces sp.
H447Q H447Q mutant shows wild-type activity in isomerization, kcat for oxidation reaction is reduced 120fold, Km increases 2fold compared to wild-type, E361Q mutant has no isomerization activity, kcat is 30fold slower than for wild-type, Glu361 may therefore act as general base in oxidation reaction Streptomyces sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.003
-
 cholesterol
-
 Streptomyces sp.
0.0275
-
 dehydroepiandrosterone
-
 Streptomyces sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cholesterol + O2 Streptomyces sp.
-
 cholest-5-en-3-one + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Streptomyces sp. P12676
-
-

Reaction

Reaction Comment Organism Reaction ID
cholesterol + O2 = cholest-5-en-3-one + H2O2 bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid Streptomyces sp.
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cholesterol + O2
-
 Streptomyces sp. cholest-4-en-3-one + H2O2
-
 ?
cholesterol + O2
-
 Streptomyces sp. cholest-5-en-3-one + H2O2
-
 ?
dehydroisoandrosterone + O2
-
 Streptomyces sp. androst-5-en-3,17-dione + H2O
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.69
-
 dehydroepiandrosterone
-
 Streptomyces sp.
44
-
 cholesterol
-
 Streptomyces sp.