title: Properties of purified squalene-hopene cyclase from Bacillus acidocaldarius.
abstract: The squalene-hopene cyclase from Bacillus acidocaldarius cytoplasmic membrane, was purified to homogeneity by solubilization with Triton X-100, chromatography on DEAE-cellulose, phenyl Sepharose and two gel-filtration columns. The enzyme monomer had a molecular mass of 75 kDa. The sequence of the first 23 amino acids was determined by Edman degradation. The enzyme activity was efficiently inhibited by n-alkyldimethylammonium halides with alkyl chain lengths between 12 and 18 C atoms. Inhibition was also observed with (5-hydroxycarvacryl)trimethylammonium chloride 1-piperidine carboxylate, dodecyldimethylamine N-oxide, azasqualene and farnesol. Competitive inhibition with dodecyltrimethylammonium bromide, (5-hydroxycarvacryl)trimethylammonium chloride 1-piperidine carboxylate and dodecyldimethylamine N-oxide was demonstrated by Lineweaver-Burk plots.
authors: Universität Tübingen, Botanisches Institut, Mikrobiologie, Federal Republic of Germany.
authors: D
authors: D
authors: Ochs
authors: C H
authors: CH
authors: Tappe
authors: P
authors: P
authors: Gärtner
authors: R
authors: R
authors: Kellner
authors: K
authors: K
authors: Poralla
mesh_terms: D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology*; D002413:Cations, Divalent / Q000494:pharmacology; D003902:Detergents / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D019751:Intramolecular Transferases; D007535:Isomerases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D013185:Squalene / Q000378:metabolism
chemical_list: D002413:Cations, Divalent; D003902:Detergents; D013185:Squalene; D007535:Isomerases; D019751:Intramolecular Transferases; C066630:squalene-hopene cyclase