Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/50354
標題: Functions of the conserved anionic amino acids and those interacting with the substrate phosphate group of phosphoglucose isomerase
作者: Meng, M.H.
孟孟孝
Lin, H.Y.
Hsieh, C.J.
Chen, Y.T.
關鍵字: phosphoglucose isomerase;glucose 6-phosphate isomerase;autocrine;motility factor;aldose-ketose isomerization;Bacillus;stearothermophilus;autocrine motility factor;nonspherocytic hemolytic-anemia;crystal-structure;glucose-6-phosphate isomerase;bacillus-stearothermophilus;6-phosphoglucose isomerase;phosphohexose;isomerase;factor neuroleukin;gpi deficiency;expression
Project: Febs Letters
期刊/報告no:: Febs Letters, Volume 499, Issue 1-2, Page(s) 11-14.
摘要: 
Phosphoglucose isomerase catalyzes the isomerization isomerization glucose 6-phosphate and fructose 6-phosphate in cytoplasm, and functions as autocrine motility factor and neuroleukin outside the tells. A phosphoglucose isomerase from Bacillus stearothermophilus (pgiA) was subjected to mutagenesis study to address the catalytic function of the conserved anionic residues and those probably interacting with the phosphate group of substrates. The results suggest that Glu290 works concertedly with His311 as a general acid-base pair to initiate the isomerization step, and Glu150 assists the base function of His311. The conserved loop structure consisting of Gly205-Gly206-Arg207 plays a critical role for the recognition of substrates. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
URI: http://hdl.handle.net/11455/50354
ISSN: 0014-5793
DOI: 10.1016/s0014-5793(01)02507-8
Appears in Collections:生物科技學研究所

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