Article
Dissecting the structural determinants of the stability of cholesterol oxidase containing covalently bound flavin.
The Journal of biological chemistry - 17 Jun 2005
Caldinelli Laura, Iametti Stefania, Barbiroli Alberto, Bonomi Francesco, Fessas Dimitrios, Molla Gianluca, Pilone Mirella S, Pollegioni Loredano
Abstract excerpt
Cholesterol oxidase from Brevibacterium sterolicum is a monomeric flavoenzyme catalyzing the oxidation and isomerization of cholesterol to cholest-4-en-3-one. This protein is a class II cholesterol oxidases, with the FAD cofactor covalently linked to the enzyme through the His(69) residue. In this work, unfolding of wild-type cholesterol oxidase was compared with that of a H69A mutant, which does not covalently...
Topics
- Anilino Naphthalenesulfonates
- Brevibacterium
- Calorimetry
- Carbon Monoxide
- Catalysis
- Cholesterol Oxidase
- Circular Dichroism
- DNA, Complementary
- Dose-Response Relationship, Drug
- Electrophoresis, Polyacrylamide Gel