Altered product pattern of a squalene-hopene cyclase by mutagenesis of active site residues

被引：43

作者：

Merkofer, T

Pale-Grosdemange, C

Wendt, KU

Rohmer, M

Poralla, K ^{[1
]}

机构：

[1] Univ Tubingen, D-72076 Tubingen, Germany

[2] Univ Strasbourg 1, Inst Le Bel, F-67070 Strasbourg, France

[3] Univ Freiburg, Inst Organ Chem & Biochem, D-79104 Freiburg, Germany

来源：

TETRAHEDRON LETTERS | 1999年 / 40卷 / 11期

关键词：

squalene cyclization; hopene; triterpene synthase;

D O I：

10.1016/S0040-4039(99)00145-8

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

Amino acid residues lining the catalytic cavity of squalene-hopene cyclase of Alicyclobacillus acidocaldarius have been mutated. Alterations of His451 to Ala and Trp489 to Ala resulted in reduced enzymatic activity, while the product patterns were identical to that of the wild-type. Mutation of Phe601 to Ala led to the enhanced formation of a tetracyclic triterpene, 17-isodammara-20(21),24-diene 4, and of Tyr420 to Ala to a significant alteration of the product pattern. (C) 1999 Published by Elsevier Science Ltd. All rights reserved.

引用

页码：2121 / 2124

页数：4

共 9 条

[1] Methodology for the preparation of pure recombinant S-cerevisiae lanosterol synthase using a Baculovirus expression system. Evidence that oxirane cleavage and A-ring formation are concerted in the biosynthesis of lanosterol from 2,3-oxidosqualene [J].