Purification and properties of the squalene-hopene cyclase from Rhodopseudomonas palustris, a purple non-sulfur bacterium producing hopanoids and tetrahymanol.
The squalene-hopene cyclase of the hopanoid- and tetrahymanol-producing Rhodopseudomonas palustris was released from the isolated membranes by CHAPS and purified to homogeneity by successive chromatography on DEAE Sephacel, Octyl Sepharose, and Blue Sepharose. The enzyme has a molecular weight of 70 kDa as determined by SDS-PAGE and an isoelectric point at about pH 5.0. The enzyme activity has a maximum at 30 degrees C and at pH 6.5. No production of tetrahymanol could be demonstrated by using either crude or purified cyclase preparations.
Kleemann
G
G
Botanisches Institut, Universität Tübingen, Germany.
Kellner
R
R
Poralla
K
K
D000595:Amino Acid Sequence; D019751:Intramolecular Transferases; D007535:Isomerases / Q000737:chemistry / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D012241:Rhodopseudomonas / Q000201:enzymology*; D014315:Triterpenes / Q000737:chemistry
D014315:Triterpenes; C100046:tetrahymanol; D007535:Isomerases; D019751:Intramolecular Transferases; C066630:squalene-hopene cyclase