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Solubilization and identification of essential functional groups of Candida albicans oxidosqualene cyclase

Medical Mycology , Volume 33 (1) – Jan 1, 1995

Details

Publisher
Informa UK Ltd
Copyright
©© 1995 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted
Subject
Original Article
ISSN
1369-3786
eISSN
1460-2709
D.O.I.
10.1080/02681219580000111
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Solubilization and identification of essential functional groups of Candida albicans oxidosqualene cyclase

Abstract

The enzyme properties and location of essential functional groups of solubilized oxidosqualene cyclase of Candida albicans have been studied. We show that the C. albicans enzyme is much more heat-labile compared with Saccharomyces cerevisiae and rat liver cyclases, requires a histidyl residue for enzyme activity, contains an essential thiol residue either close to or in the active site and exhibits a carbocationic mechanism for catalysis, as the enzyme-bound substrate protects the enzyme from inactivation by a site-directed inactivator.
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