Purification and properties of the squalene-hopene cyclase from Rhodopseudomonas palustris, a purple non-sulfur bacterium producing hopanoids and tetrahymanol

Biochim Biophys Acta. 1994 Jan 20;1210(3):317-20. doi: 10.1016/0005-2760(94)90235-6.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Intramolecular Transferases*
  • Isomerases / chemistry
  • Isomerases / isolation & purification*
  • Molecular Sequence Data
  • Rhodopseudomonas / enzymology*
  • Triterpenes / chemistry

Substances

  • Triterpenes
  • tetrahymanol
  • Isomerases
  • Intramolecular Transferases
  • squalene-hopene cyclase