Isolation of the dxr gene of Zymomonas mobilis and characterization of the 1-deoxy-D-xylulose 5-phosphate reductoisomerase

被引：40

作者：

Grolle, S ^{[1
]}

Bringer-Meyer, S ^{[1
]}

Sahm, H ^{[1
]}

机构：

[1] Forschungszentrum Julich, Inst Biotechnol 1, D-52425 Julich, Germany

来源：

FEMS MICROBIOLOGY LETTERS | 2000年 / 191卷 / 01期

关键词：

1-deoxy-D-xylulose 5-phosphate reductoisomerase; 2C-methyl-D-erythritol 4-phosphate pathway; isoprenoid biosynthesis; Zymomonas mobilis;

D O I：

10.1016/S0378-1097(00)00382-7

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The gene encoding the second enzyme of the 2C-methyl-D-erythritol 4-phosphate (MEP) pathway for isopentenyl diphosphate biosynthesis, 1-deoxy-D-xylulose 5-phosphate (DXP) reductoisomerase, was cloned and sequenced from Zymomonas mobilis. The deduced amino acid sequence showed the highest identity (48.2%) to the DXP reductoisomerase of Escherichia coli. Biochemical characterization of the purified DXP reductoisomerase showed a strict dependence of the enzyme on NADPH and divalent cations (Mn2+, Co2+ or Mg2+). The enzyme is a dimer with a molecular mass of 39 kDa per subunit and has a specific activity of 19.5 U mg protein(-1). Catalysis of the intramolecular rearrangement and reduction of DXP to MEP is competitively inhibited by the antibiotic fosmidomycin with a K-i of 0.6 mu.M. (C) 2000 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：131 / 137

页数：7

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