LytB protein catalyzes the terminal step of the 2-C-methyl-D-erythritol-4-phosphate pathway of isoprenoid biosynthesis

被引：127

作者：

Altincicek, B

Duin, EC

Reichenberg, A

Hedderich, R

Kollas, AK

Hintz, M

Wagner, S

Wiesner, J

Beck, E

Jomaa, H

机构：

[1] Jomaa Pharmaka GMBH, D-35392 Giessen, Germany

[2] Max Planck Inst Terr Mikrobiol, D-35043 Marburg, Germany

[3] Univ Giessen, Inst Biochem, D-35392 Giessen, Germany

来源：

FEBS LETTERS | 2002年 / 532卷 / 03期

关键词：

isoprenoid biosynthesis; 2-C-methyl-D-erythritol-4-phosphate pathway; LytB;

D O I：

10.1016/S0014-5793(02)03726-2

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：

Recombinant LytB protein from the thermophilic eubacterium Aquifex aeolicus produced in Escherichia coli was purified to apparent homogeneity. The purified LytB protein catalyzed the reduction of (E)-4-hydroxy-3-methyl-but-2-enyI diphosphate (HMBPP) in a defined in vitro system. The reaction products were identified as isopentenyl diphosphate and dimethylallyl diphosphate. A spectrophotometric assay was established to determine the steady-state kinetic parameters of LytB protein. The maximal specific activity of 6.6 +/- 0.3 mumol min(-1) mg(-1) protein was determined at pH 7.5 and 60degreesC. The k(cat) value of the LytB protein was 3.7 +/- 0.2 s(-1) and the K-m value for HMBPP was 590 +/- 60 muM. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：437 / 440

页数：4

共 11 条

[1] Biosynthesis of terpenes:: Studies on 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase [J].