Structures, mechanisms and inhibitors of undecaprenyl diphosphate synthase: A cis-prenyltransferase for bacterial peptidoglycan biosynthesis

被引：31

作者：

Teng, Kuo-Hsun ^{[1
]}

Liang, Po-Huang ^{[1
]}

机构：

[1] Acad Sinica, Inst Biol Chem, Taipei 11529, Taiwan

来源：

BIOORGANIC CHEMISTRY | 2012年 / 43卷

关键词：

Isoprenoid; Prenyltransferase; X-ray structure; Pre-steady-state kinetics; Conformational change; Inhibitor; OCTAPRENYL PYROPHOSPHATE SYNTHASE; CHAIN-LENGTH DETERMINATION; STATE KINETIC-ANALYSIS; CRYSTAL-STRUCTURE; PROTEIN FARNESYLTRANSFERASE; MOLECULAR-CLONING; AROMATIC PRENYLTRANSFERASE; TRANS-PRENYLTRANSFERASES; SACCHAROMYCES-CEREVISIAE; CONFORMATIONAL-CHANGE;

D O I：

10.1016/j.bioorg.2011.09.004

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：

Isoprenoids are an intensive group of compounds made from isopentenyl diphosphate (IPP), catalyzed by prenyltransferases such as farnesyl diphosphate (FPP) cyclases, squalene synthase, protein farnesyltransferases and geranylgeranyltransferases, aromatic prenyltransferases as well as a group of prenyltransferases (cis- and trans-types) catalyzing consecutive condensation reactions of FPP with specific numbers of IPP to generate linear products with designate chain lengths. These prenyltransferases play significant biological functions and some of them are drug targets. In this review, structures, mechanisms, and inhibitors of a cis-prenyltransferase, undecaprenyl diphosphate synthase (UPPS) that mediates bacterial peptidoglycan biosynthesis, are summarized for comparison with the most related trans-prenyltransferases and other prenyltransferases. (C) 2011 Elsevier Inc. All rights reserved.

引用

页码：51 / 57

页数：7

共 68 条

[31] Evolution of aromatic prenyltransferases in the biosynthesis of indole derivatives [J].