title: 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.
authors.affiliation: Lepetit Research Center, Marion Merrell Dow Research Institute, Gerenzano (Va), Italy.
authors.forename: L
authors.initials: L
authors.lastname: Carrano
authors.forename: M
authors.initials: M
authors.lastname: Noe
authors.forename: G
authors.initials: G
authors.lastname: Grosa
authors.forename: P
authors.initials: P
authors.lastname: Milla
authors.forename: M
authors.initials: M
authors.lastname: Denaro
authors.forename: K
authors.initials: K
authors.lastname: Islam
mesh_terms: D000818:Animals; D002176:Candida albicans / Q000201:enzymology*; D019751:Intramolecular Transferases; D007535:Isomerases / Q000737:chemistry* / Q000302:isolation & purification*; D008861:Microsomes / Q000201:enzymology; D008862:Microsomes, Liver / Q000201:enzymology; D051381:Rats; D012441:Saccharomyces cerevisiae / Q000201:enzymology
chemical_list: D007535:Isomerases; D019751:Intramolecular Transferases; C021924:lanosterol synthase