This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Cholesterol oxidase
From Proteopedia
(Difference between revisions)
| Line 8: | Line 8: | ||
== Function == | == Function == | ||
| - | '''Cholesterol oxidase''' (COX) catalyzes the conversion of cholesterol and molecular oxygen to Colest-4-en-3-one and hydrogen peroxide. COX uses FAD as a cofactor. '''COX I''' binds FAD non-covalently whereas '''COX II''' binds FAD covalently.<ref>PMID: | + | '''Cholesterol oxidase''' (COX) catalyzes the conversion of cholesterol and molecular oxygen to Colest-4-en-3-one and hydrogen peroxide. COX uses FAD as a cofactor. '''COX I''' binds FAD non-covalently whereas '''COX II''' binds FAD covalently.<ref>PMID:20102741</ref> |
== Relevance == | == Relevance == | ||
Revision as of 11:43, 7 December 2015
| |||||||||||
3D structure of cholesterol oxidase
Updated on 07-December-2015
References
- ↑ Sagermann M, Ohtaki A, Newton K, Doukyu N. Structural characterization of the organic solvent-stable cholesterol oxidase from Chromobacterium sp. DS-1. J Struct Biol. 2010 Apr;170(1):32-40. Epub 2010 Jan 25. PMID:20102741 doi:10.1016/j.jsb.2010.01.012
