Cloning and functional analysis of cis-prenyltransferase from Thermobifida fusca

被引：4

作者：

Ambo, Takanori ^{[1
]}

Noike, Motoyoshi ^{[1
]}

Kurokawa, Hirofumi ^{[1
]}

Koyama, Tanetoshi ^{[1
]}

机构：

[1] Tohoku Univ, Inst Multidisciplinary Res Adv Mat, Aoba Ku, Sendai, Miyagi 9808577, Japan

来源：

JOURNAL OF BIOSCIENCE AND BIOENGINEERING | 2009年 / 107卷 / 06期

关键词：

Sugar carrier lipid biosynthesis; Prenyltransferase; Thermobifida fusca; Actinomycete; Isoprenoid biosynthesis; UNDECAPRENYL DIPHOSPHATE SYNTHASE; PRODUCT CHAIN-LENGTH; MICROCOCCUS-LUTEUS B-P-26; MYCOBACTERIUM-TUBERCULOSIS; DETERMINATION MECHANISM; ELONGATING ENZYMES; SUBSTRATE-BINDING; CRYSTAL-STRUCTURE; IDENTIFICATION; PURIFICATION;

D O I：

10.1016/j.jbiosc.2009.02.006

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

cis-Prenyltransferase catalyzes the synthesis of Z,E-mixed prenyl diphosphates by a condensation of isopentenyl diphosphate to an allylic diphosphate. A novel gene encoding a cis-prenyltransferase is cloned from Thermobifida fusca. It showed a unique substrate specificity accepting dimethylallyl diphosphate as a shortest allylic substrate, and synthesizes polyprenyl products up to C-70. (C) 2009, The Society for Biotechnology, Japan. All rights reserved.

引用

页码：620 / 622

页数：3

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