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Bifunctional phosphomannose isomerase/GDP‐ D ‐mannose pyrophosphorylase is the point of control for GDP‐ D ‐mannose biosynthesis in Helicobacter pylori
Author(s) -
Wu Bingyuan,
Zhang Yingxin,
Zheng Rong,
Guo Cuiwen,
Wang Peng George
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02717-5
Subject(s) - mannose , biosynthesis , biochemistry , chemistry , isomerase , phosphofructokinase 2 , enzyme , fructose
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.