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Literature summary for 1.1.3.6 extracted from

  • Qin, H.M.; Wang, J.W.; Guo, Q.; Li, S.; Xu, P.; Zhu, Z.; Sun, D.; Lu, F.
    Refolding of a novel cholesterol oxidase from Pimelobacter simplex reveals dehydrogenation activity (2017), Protein Expr. Purif., 139, 1-7 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Pimelobacter simplex

Organism

Organism UniProt Comment Textmining
Pimelobacter simplex A0A0A1DJ35
-
-

Purification (Commentary)

Purification (Comment) Organism
effective method for the preparation of active PsChO3 using urea as denaturing agent, combined with his-tag trapping and on-column refolding. Using this method, the enzyme is successfully refolded from inclusion bodies expressed in Escherichia coli Pimelobacter simplex

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cholesterol + O2
-
Pimelobacter simplex cholest-5-en-3-one + H2O2
-
?

Synonyms

Synonyms Comment Organism
ChO3
-
Pimelobacter simplex

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
Pimelobacter simplex

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 45 25°C: about 85% of maximal activity, 45°C: about 40% of maximal activity Pimelobacter simplex

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Pimelobacter simplex

pH Range

pH Minimum pH Maximum Comment Organism
6.5 9 pH 6.5: about 50% of maximal activity, pH 9.0: about 50% of maximal activity Pimelobacter simplex