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The Folding of Squalene; An Old Problem has New Results
Author(s) -
Bohlmann Rolf
Publication year - 1992
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199205821
Subject(s) - lanosterol , biogenesis , squalene , context (archaeology) , enzyme , folding (dsp implementation) , chemistry , stereochemistry , sterol , steroid , biochemistry , computational biology , biology , cholesterol , engineering , electrical engineering , paleontology , hormone , gene
For the recognition of new applications of steroids , basic research is essential—‐ especially when the desired effects are unprecedented in nature. In this context the recent reports by Corey et al. on the biogenesis of sterols is important. The enzyme sterolcyclase, which catalyzes the fourfold cyclization of the 2,3‐epoxide‐oxidosqualene ( 1 ) to lanosterol thus constructing the steroid framework in one step, can only now be purified. Once purified, the enzyme can be stored at 0°C for at least 14 days without loss of activity. Thus, further in‐depth investigations into mechanistic aspects and the structure of the enzyme are now possible.