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Literature summary extracted from

  • Chen, L.; Lyubimov, A.Y.; Brammer, L.; Vrielink, A.; Sampson, N.S.
    The binding and release of oxygen and hydrogen peroxide are directed by a hydrophobic tunnel in cholesterol oxidase (2008), Biochemistry, 47, 5368-5377.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.3.6 structure of the F359W mutant enzyme, hanging drop vapor diffusion method. In the atomic-resolution structure of F359W, the indole ring of the tryptophan completely fills the tunnel and is observed in only a single conformation Streptomyces sp.

Protein Variants

EC Number Protein Variants Comment Organism
1.1.3.6 F359W kcat for the F359W mutant-catalyzed reaction decreases 13fold relative to that of the wild-type-catalyzed reaction. Transfer of hydride from the sterol to the flavin prosthetic group is no longer rate-limiting for the mutant enzyme. Kinetic cooperativity with respect to molecular oxygen is observed with the tunnel mutant, but not with the wild-type enzyme. In the atomic-resolution structure of F359W, the indole ring of the tryptophan completely fills the tunnel and is observed in only a single conformation. The size of the indole is proposed to limit conformational rearrangement of residue 359 that leads to tunnel opening in the wild-type enzyme Streptomyces sp.
1.1.3.6 G347N mutant can not be saturated with oxygen. Transfer of hydride from the sterol to the flavin prosthetic group is no longer rate-limiting for the mutant enzyme. Kinetic cooperativity with respect to molecular oxygen is observed with the tunnel mutant, but not with the wild-type enzyme Streptomyces sp.
1.1.3.6 N485D mutant can not be saturated with oxygen. Transfer of hydride from the sterol to the flavin prosthetic group is no longer rate-limiting for the mutant enzyme. Kinetic cooperativity with respect to molecular oxygen is observed with the tunnel mutant, but not with the wild-type enzyme Streptomyces sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.3.6 O2
-
 Streptomyces sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.6 0.0015
-
 cholesterol mutant enzyme G347N, determined by cholest-4-en-3-one detection Streptomyces sp.
1.1.3.6 0.0027
-
 cholesterol mutant enzyme F359W, determined by cholest-4-en-3-one detection Streptomyces sp.
1.1.3.6 0.0027
-
 cholesterol wild-type enzyme, determined by cholest-4-en-3-one detection Streptomyces sp.
1.1.3.6 0.0027
-
 cholesterol wild-type enzyme, determined by H2O2 detection Streptomyces sp.
1.1.3.6 0.004
-
 cholesterol mutant enzyme F359W, determined by H2O2 detection Streptomyces sp.
1.1.3.6 0.005
-
 cholesterol mutant enzyme G347N, determined by H2O2 detection Streptomyces sp.
1.1.3.6 0.0062
-
 cholesterol mutant enzyme N485D, determined by H2O2 detection Streptomyces sp.
1.1.3.6 0.007
-
 cholesterol mutant enzyme N485D, determined by cholest-4-en-3-one detection Streptomyces sp.
1.1.3.6 0.3
-
 O2 wild-type enzyme Streptomyces sp.
1.1.3.6 0.617
-
 O2 mutant enzyme F359W Streptomyces sp.

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.6 Streptomyces sp. P12676
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.3.6
-
 Streptomyces sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.6 cholesterol + O2
-
 Streptomyces sp. cholest-4-en-3-one + H2O2
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.3.6 0.035
-
 cholesterol mutant enzyme N485D, determined by H2O2 detection Streptomyces sp.
1.1.3.6 0.073
-
 cholesterol mutant enzyme N485D, determined by cholest-4-en-3-one detection Streptomyces sp.
1.1.3.6 0.85
-
 cholesterol mutant enzyme G347N, determined by H2O2 detection Streptomyces sp.
1.1.3.6 0.86
-
 cholesterol mutant enzyme F359W, determined by cholest-4-en-3-one detection Streptomyces sp.
1.1.3.6 1
-
 cholesterol mutant enzyme G347N, determined by cholest-4-en-3-one detection Streptomyces sp.
1.1.3.6 1.3
-
 cholesterol mutant enzyme F359W, determined by H2O2 detection Streptomyces sp.
1.1.3.6 42
-
 cholesterol wild-type enzyme, determined by cholest-4-en-3-one detection Streptomyces sp.
1.1.3.6 47
-
 cholesterol wild-type enzyme, determined by H2O2 detection Streptomyces sp.

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.3.6 1.381
-
 O2 mutant enzyme F359W Streptomyces sp.
1.1.3.6 1.383
-
 O2 wild-type enzyme Streptomyces sp.