Cholesterol Oxidase from Brevibacterium sterolicum
نویسندگان
چکیده
منابع مشابه
Characterization of cholesterol oxidase from Streptomyces hygroscopicus and Brevibacterium sterolicum.
The FAD-containing enzyme cholesterol oxidase catalyzes the oxidation and isomerization of 3beta-hydroxysteroids having a trans double bond at delta5-delta6 of the steroid ring backbone to the corresponding delta4-3-ketosteroid. Two representative enzymes of this family, namely cholesterol oxidase from Streptomyces hygroscopicus (SCO) and the recombinant enzyme from Brevibacterium sterolicum (B...
متن کاملCholesterol oxidase from Streptomyces hygroscopicus and Brevibacterium sterolicum: effect of surfactants and organic solvents on activity.
We have studied systematically the effect of the non-ionic surfactants Thesit and Triton X-100, and of propan-2-ol (used as a substrate solubilizer) on the activity of the cholesterol oxidases from Streptomyces hygroscopicus (SCO) and Brevibacterium sterolicum (BCO). Low concentrations of Thesit lead to an activity increase with both enzymes; at higher surfactant concentrations the opposite eff...
متن کاملCholesterol oxidase from Brevibacterium sterolicum. The relationship between covalent flavinylation and redox properties.
Brevibacterium sterolicum possesses two forms of cholesterol oxidase, one containing noncovalently bound FAD, the second containing a FAD covalently linked to His(69) of the protein backbone. The functional role of the histidyl-FAD bond in the latter cholesterol oxidase was addressed by studying the properties of the H69A mutant in which the FAD is bound tightly, but not covalently, and by comp...
متن کاملKinetic mechanisms of cholesterol oxidase from Streptomyces hygroscopicus and Brevibacterium sterolicum.
The kinetic properties of two cholesterol oxidases, one from Brevibacterium sterolicum (BCO) the other from Streptomyces hygroscopicus (SCO) were investigated. BCO works via a ping-pong mechanism, whereas the catalytic pathway of SCO is sequential. The turnover numbers at infinite cholesterol and oxygen concentrations are 202 s-1 and 105 s-1 for SCO and BCO, respectively. The rates of flavin re...
متن کاملCholesterol oxidase from Brevibacterium sterolicum and Streptomyces hygroscopicus : a covalent FAD binding vs. a non-covalent one
Introduction Cholesterol oxidase (CO, EC 1.1.3.6) is a flavoenzyme which catalyzes the first step in the pathway of cholesterol degradation in various microorganisms. CO is a bifunctional enzyme: it catalyzes the oxidation of ß-hydroxysteroids and the isomerization of the produced [\s-ketosteroid to the [\4-3-ketosteroid. The three dimensional structure of CO from Brevibacterium, which contains...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2001
ISSN: 0021-9258
DOI: 10.1074/jbc.m010953200