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- Title
Identification of amino acid residues important for the phosphomannose isomerase activity of PslB in Pseudomonas aeruginosa PAO1
- Authors
Lee, Hui-Ju; Chang, Hwan-You; Venkatesan, Nandinin; Peng, Hwei-Ling
- Abstract
Abstract: 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 K M 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.
- Subjects
AMINO acids; ISOMERASES; PSEUDOMONAS aeruginosa; MANNOSE
- Publication
FEBS Letters, 2008, Vol 582, Issue 23/24, p3479
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2008.09.013