Squalene-hopene cyclase: catalytic mechanism and substrate recognition

Chem Commun (Camb). 2002 Feb 21:(4):291-301. doi: 10.1039/b108995c.

Abstract

Rapid progress on the catalytic mechanism and substrate recognition by squalene-hopene cyclase, which has occurred only in the last several years, is reported. A series of site-directed mutation experiments and some squalene analogues have provided deep insight into the polycyclization mechanism and catalytic sites in conjunction with the information from X-ray crystal data.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carbohydrate Sequence
  • Catalysis
  • Crystallography, X-Ray
  • Cyclization
  • Gram-Positive Endospore-Forming Rods / enzymology
  • Gram-Positive Endospore-Forming Rods / genetics
  • Intramolecular Transferases / genetics
  • Intramolecular Transferases / metabolism*
  • Kinetics
  • Molecular Sequence Data
  • Mutation / genetics
  • Protein Conformation
  • Substrate Specificity
  • Tetrahymena pyriformis / genetics

Substances

  • Intramolecular Transferases
  • squalene-hopene cyclase