Identification of amino acid residues important for the phosphomannose isomerase activity of PslB in Pseudomonas aeruginosa PAO1

Hui Ju Lee, Hwan You Chang, Nandinin Venkatesan, Hwei-Ling Peng*

*Corresponding author for this work

研究成果: Article

10 引文 斯高帕斯(Scopus)

摘要

Phosphomannose isomerase (PMI) plays a pivotal role in biosynthesis of GDP-mannose, an important precursor of many polysaccharides. We demonstrate in this study that Pseudomonas aeruginosa pslB encodes a protein with GDP-mannose pyrophosphorylase/PMI dual activities. The PMI activity is Co2+-dependent and could be inhibited by GDP-mannose in a competitive manner. Furthermore, the activity could be inactivated by 2,3-butanedione suggesting the presence of a catalytic Arg residue. Site-specific mutations at R373, R472, R479, E410, H411, N433 and E458 increase the KM approximately 8-20-fold. The PMI activity of PslB was completely diminished with a R408K or R408A, reflecting the importance of this residue in catalysis. Overall, these results provide a basis for understanding the catalytic mechanism of PMI.

原文English
頁(從 - 到)3479-3483
頁數5
期刊FEBS Letters
582
發行號23-24
DOIs
出版狀態Published - 15 十月 2008

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