Isopentenyl diphosphate isomerase: A checkpoint to isoprenoid biosynthesis

被引：133

作者：

Berthelot, Karine ^{[1
]}

Estevez, Yannick ^{[1
]}

Deffieux, Alain ^{[1
]}

Peruch, Frederic ^{[1
]}

机构：

[1] ENSCBP, IPB, UMR 5629, Lab Chim Polymeres Organ,CNRS, F-33607 Pessac, France

来源：

BIOCHIMIE | 2012年 / 94卷 / 08期

关键词：

Isopentenyl diphosphate isomerase; IPP; DMAPP; Isoprenoid synthesis; Terpens; PYROPHOSPHATE ISOMERASE; ESCHERICHIA-COLI; CRYSTAL-STRUCTURE; FUNCTIONAL-ANALYSIS; MEVALONATE PATHWAY; CAROTENOID BIOSYNTHESIS; THERMUS-THERMOPHILUS; PARTIAL-PURIFICATION; CATALYTIC MECHANISM; BACILLUS-SUBTILIS;

D O I：

10.1016/j.biochi.2012.03.021

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：

Even if the isopentenyl diphosphate (IPP) isomerases have been discovered in the 50s, it is only in the last decade that the genetical, enzymatical, structural richness and cellular importance of this large family of crucial enzymes has been uncovered. Present in all living kingdoms, they can be classified in two subfamilies: type 1 and type 2 IPP isomerases, which show clearly distinct characteristics. They all perform the regulatory isomerization of isopentenyl diphosphate into dimethylallyl diphosphate, a key rate-limiting step of the terpenoid biosynthesis, via a protonation/deprotonation mechanism. Due to their importance in the isoprenoid metabolism and the increasing interest of industry devoted to terpenoid production, it is foreseen that the biotechnological development of such enzymes should be under intense scrutiny in the near future. (C) 2012 Elsevier Masson SAS. All rights reserved.

引用

页码：1621 / 1634

页数：14

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