Bifunctional phosphomannose isomerase/GDP‐D‐mannose pyrophosphorylase is the point of control for GDP‐D‐mannose biosynthesis in Helicobacter pylori

FEBS Letters

Guo, Cuiwen¹  Zheng, Rong¹  Zhang, Yingxin¹  Wang, Peng George¹  Wu, Bingyuan¹ 

[1] Department of Chemistry, Wayne State University, Detroit, MI 48202, USA

关键词: Phosphomannose isomerase/GDP-D-mannose pyrophosphorylase;    GDP-D-mannose;    Feedback inhibition;    Helicobacter pylori;    DTT;    dithiothreitol;    F6P;    D-fructose-6-phosphate;    GMP;    GDP-D-mannose pyrophosphorylase;    IPTG;    isopropyl-D-thiogalactopyranoside;    M1P;    D-mannose-1-phosphate;    M6P;    D-mannose-6-phosphate;    NADP+;    nicotinamide adenine dinucleotide phosphate;    PMI;    phosphomannose isomerase;    PMI/GMP;    bifunctional phosphomannose isomerase/GDP-D-mannose pyrophosphorylase;    PMM;    phosphomannomutase;    Ppi;    inorganic pyrophosphate;   

DOI  :  10.1016/S0014-5793(02)02717-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In this report a recombinant bifunctional phosphomannose isomerase/GDP-D-mannose pyrophosphorylase from Helicobacter pylori has been studied. The enzyme catalyzes the first and third steps of GDP-D-mannose biosynthesis from D-fructose-6-phosphate. The first step, isomerization from D-fructose-6-phosphate to D-mannose-6-phosphate, is found to be rate-limiting in GDP-D-mannose biosynthesis due to feedback inhibition. The inhibition is of non-competitive (mixed) type. As the enzyme is found only in bacteria probably participating in capsular polysaccharide biosynthesis, it could be a specific therapeutic target against bacterial infection.

【 授权许可】

Unknown