Taxadiene synthase structure and evolution of modular architecture in terpene biosynthesis

被引：0

作者：

Mustafa Köksal

Yinghua Jin

Robert M. Coates

Rodney Croteau

David W. Christianson

机构：

[1] Roy and Diana Vagelos Laboratories,Department of Chemistry

[2] University of Pennsylvania,Department of Chemistry

[3] 231 South 34th Street,Department of Chemistry and Biochemistry

[4] Philadelphia,undefined

[5] Pennsylvania 19104-6323,undefined

[6] USA,undefined

[7] University of Illinois at Urbana-Champaign,undefined

[8] University of Colorado,undefined

[9] Institute of Biological Chemistry,undefined

[10] Washington State University,undefined

来源：

Nature | 2011年 / 469卷

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摘要：

The first step in the biosynthesis of the anticancer compound Taxol (paclitaxel) and many other natural C20 diterpenes is the cyclization of an isoprenoid, catalysed by taxadiene synthase. The X-ray crystal structure of this enzyme from the Pacific yew has now been determined. Its C-terminal catalytic domain binds and activates the substrate in a manner seen in class I terpenoid cyclases, but the N-terminal domain and a third 'insertion' domain adopt the fold of a class II terpenoid cyclase. This suggests that this enzyme could be the ancestral progenitor of all terpenoid cyclases.

引用

页码：116 / 120

页数：4

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