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Journal of Bacteriology logoLink to Journal of Bacteriology
. 1992 Jan;174(1):298–302. doi: 10.1128/jb.174.1.298-302.1992

Cloning, expression, and sequencing of squalene-hopene cyclase, a key enzyme in triterpenoid metabolism.

D Ochs 1, C Kaletta 1, K D Entian 1, A Beck-Sickinger 1, K Poralla 1
PMCID: PMC205708  PMID: 1729216

Abstract

The pentacyclic hopanoids, a class of eubacterial lipids, are synthesized by squalene-hopene cyclase and side chain-elongating enzymes. With the aid of DNA probes based on the amino-terminal sequence of purified squalene-hopene cyclase from Bacillus acidocaldarius, clones of Escherichia coli that express this enzyme in the cytoplasmic membrane were isolated. According to the DNA sequence, the cyclase contained 627 amino acids with a molecular mass of 69,473 Da. A high percentage of the amino acids were basic. No significant similarity to existing sequenced proteins was found.

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Selected References

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