RRC ID 4920
Author Desai KK, Miller BG.
Title A metabolic bypass of the triosephosphate isomerase reaction.
Journal Biochemistry
Abstract Triosephosphate isomerase (TIM) catalyzes the interconversion of d-glyceraldehyde 3-phosphate and dihydroxyacetone phosphate, an essential step in glycolytic and gluconeogenic metabolism. To uncover promiscuous isomerases embedded within the Escherichia coli genome, we searched for genes capable of restoring growth of a TIM-deficient bacterium under gluconeogenic conditions. Rather than discovering an isomerase, we selected yghZ, a gene encoding a member of the aldo-keto reductase superfamily. Here we show that YghZ catalyzes the stereospecific, NADPH-dependent reduction of l-glyceraldehyde 3-phosphate, the enantiomer of the TIM substrate. This transformation provides an alternate pathway to the formation of dihydroxyacetone phosphate.
Volume 47(31)
Pages 7983-5
Published 2008-8-5
DOI 10.1021/bi801054v
PMID 18620424
MeSH Alcohol Oxidoreductases / genetics Alcohol Oxidoreductases / metabolism Aldehyde Reductase Aldo-Keto Reductases Catalysis Dihydroxyacetone Phosphate / chemistry Dihydroxyacetone Phosphate / metabolism Escherichia coli / enzymology Escherichia coli / genetics Escherichia coli / metabolism Escherichia coli Proteins / genetics Escherichia coli Proteins / metabolism* Glyceraldehyde 3-Phosphate / chemistry Glyceraldehyde 3-Phosphate / metabolism Models, Biological Stereoisomerism Substrate Specificity Sugar Phosphates / chemistry Sugar Phosphates / metabolism* Triose-Phosphate Isomerase / genetics Triose-Phosphate Isomerase / metabolism* Trioses / metabolism
IF 2.865
Times Cited 16
WOS Category BIOCHEMISTRY & MOLECULAR BIOLOGY
Resource
Prokaryotes E. coli ASKA