Change of product specificity of hexaprenyl diphosphate synthase from Sulfolobus solfataricus by introducing mimetic mutations

被引：5

作者：

Hemmi, H ^{[1
]}

Noike, M ^{[1
]}

Nakayama, T ^{[1
]}

Nishino, T ^{[1
]}

机构：

[1] Tohoku Univ, Grad Sch Engn, Dept Biochem & Engn, Sendai, Miyagi 9808579, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2002年 / 297卷 / 05期

关键词：

prenyltransferase; prenyl diphosphate synthase; hexaprenyl diphosphate synthase; archaeal enzyme; isoprenoid; terpenoid; mutagenesis; mimetic mutation; chain-length determination; evolution;

D O I：

10.1016/S0006-291X(02)02348-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The introduction of several sets of amino acid substitutions into the region around a substrate-binding site of a medium-chain (all-E) prenyl diphosphate synthase, hexaprenyl diphosphate synthase from a thermoacidophilic archaeon Sulfolobus solfataricus, to mimic the product determination mechanisms of various kinds of short-chain enzymes revealed that the structure around the region of the medium-chain enzyme resembles those of eukaryotic farnesyl diphosphate synthases but not those of the other short-chain enzymes, reflecting the evolutional relationships among these enzymes. (C) 2002 Elsevier Science (USA). All rights reserved.

引用

页码：1096 / 1101

页数：6

共 19 条

[1] Interaction with the small subunit of geranyl diphosphate synthase modifies the chain length specificity of geranylgeranyl diphosphate synthase to produce geranyl diphosphate [J].