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Literature summary for 1.1.3.6 extracted from

  • Yin, Y.; Liu, P.; Anderson, R.G.; Sampson, N.S.
    Construction of a catalytically inactive cholesterol oxidase mutant: investigation of the interplay between active site-residues glutamate 361 and histidine 447 (2002), Arch. Biochem. Biophys., 402, 235-242.
    View publication on PubMed
Search for more literature for 1.1.3.6

Protein Variants

Protein Variants Comment Organism
E361Q turnover number for cholesterol is decreased 31.4fold compared to wild-type enzyme, 1.8fold increase in Km-value for cholesterol compared to wild-type enzyme Streptomyces sp.
H447E turnover number for cholesterol is decreased about 2600fold compared to wild-type enzyme Streptomyces sp.
H447E/E361Q turnover number for cholesterol is decreased about 31500fold compared to wild-type enzyme. Mutant enzyme is not able to isomerize cholest-5-en-3-one. Mutant enzyme is folded like native enzyme and still associates with model membranes Streptomyces sp.
H447Q turnover number for cholesterol is decreased 137.5fold compared to wild-type enzyme, Km-value for cholesterol is identical to wild-type value Streptomyces sp.
H447Q/E361Q turnover number for cholesterol is decreased 473fold compared to wild-type enzyme, 1.7fold increase in Km-value for cholesterol compared to wild-type enzyme. Mutant enzyme is not able to isomerize cholest-5-en-3-one Streptomyces sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.003
-
 cholesterol wild-type enzyme Streptomyces sp.
0.003
-
 cholesterol mutant enzyme H447Q Streptomyces sp.
0.005
-
 cholesterol mutant enzyme H447Q/E361Q Streptomyces sp.
0.0054
-
 cholesterol mutant enzyme E361 Streptomyces sp.

Organism

Organism UniProt Comment Textmining
Streptomyces sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant enzymes Streptomyces sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cholesterol + O2
-
 Streptomyces sp. cholest-5-en-3-one + H2O2 subsequent isomerization to cholest-4-en-3-one ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0014
-
 cholesterol mutant enzyme H447E/E361Q Streptomyces sp.
0.017
-
 cholesterol mutant enzyme H447E Streptomyces sp.
0.093
-
 cholesterol mutant enzyme H447Q/E361Q Streptomyces sp.
0.32
-
 cholesterol mutant enzyme H447Q Streptomyces sp.
1.4
-
 cholesterol mutant enzyme E361 Streptomyces sp.
44
-
 cholesterol wild-type enzyme Streptomyces sp.