Work

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

Year: 2002

Type: article

Abstract: 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.

Source: FEBS Letters

DOI: 10.1016/s0014-5793(02)02717-5

Authors: Bingyuan Wu, Yingxin Zhang, Rong Zheng, Cuiwen Guo, Peng George Wang

Institution: Wayne State University

Language: English

Topic: Carbohydrate Chemistry and Synthesis

Subfield: Organic Chemistry

Field: Chemistry

Domain: Physical Sciences

SDG: Good health and well-being

Open Access status: bronze

OpenAlex ID: W2085771741

FWCI: 1.226

Cites: 33

Cited by: 51

Related to: 10