Open AccessProperties of purified squalene‐hopene cyclase from Bacillus acidocaldarius
Author(s) -
OCHS Dietmar,
TAPPE Cord H.,
GÄRTNER Peter,
KELLNER Roland,
PORALLA Karl
Publication year - 1990
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1990.tb19429.x
Subject(s) - chemistry , size exclusion chromatography , piperidine , chromatography , bromide , carboxylate , stereochemistry , edman degradation , organic chemistry , enzyme , biochemistry , peptide sequence , gene
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.