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Oxidosqualene Cyclase Second‐Sphere Residues Profoundly Influence the Product Profile
Author(s) -
Lodeiro Silvia,
Segura Michael J. R.,
Stahl Martin,
SchulzGasch Tanja,
Matsuda Seiichi P. T.
Publication year - 2004
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200400086
Subject(s) - cycloartenol , residue (chemistry) , chemistry , stereochemistry , cyclase , biochemistry , enzyme , sterol , cholesterol
Cycloartenol synthase converts oxidosqualene to the pentacyclic triterpene alcohol cycloartenol. Mutations at His477 dramatically alter the product profile. However, these changes are catalytically irrelevant in the presence of Tyr410Thr and Ile481Val mutations. Modeling studies have established that His477 is a second‐sphere residue that affects catalysis indirectly through its interactions with the active‐site residue Tyr410.