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Triose-phosphate isomerase (TPI or TIM) is an enzyme (EC 5.3.1.1) that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate.
Triosephosphate isomerase is an enzyme that in humans is encoded by the TPI1 gene. This gene encodes an enzyme, consisting of two identical proteins, which catalyzes the isomerization of glyceraldehyde 3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP) in glycolysis and gluconeogenesis. Mutations in this gene are associated with ...
Glyceraldehyde 3-phosphate, also known as triose phosphate or 3-phosphoglyceraldehyde and abbreviated as G3P, GA3P, GADP, GAP, TP, GALP or PGAL, is a metabolite that occurs as an intermediate in several central pathways of all organisms. [2] [3] With the chemical formula H(O)CCH(OH)CH 2 OPO 3 2-, this anion is a monophosphate ester of ...
Thirteen different mutations in the respective gene, which is located at chromosome 12p13 and encodes the ubiquitous housekeeping enzyme triosephosphate isomerase (TPI), have been discovered so far. [4] TPI is a crucial enzyme of glycolysis and catalyzes the interconversion of dihydroxyacetone phosphate and glyceraldehyde-3-phosphate.
The usual pathway converting GAP to pyruvate starts with the enzyme glyceraldehyde 3-phosphate dehydrogenase (Weber 711–13). Low phosphate levels inhibit GAP dehydrogenase; GAP is instead converted into DHAP by triosephosphate isomerase. Again, increased levels of DHAP activate methylglyoxal synthase and methylglyoxal production (Weber 711–13).
[3] Fig. 1. Schematic overview of fermentative and oxidative glucose metabolism of Saccharomyces cerevisiae. (A) upper part of glycolysis, which includes two sugar phosphorylation reactions. (B) fructose-1,6-bisphosphate aldolase, splitting the C6-molecule into two triose phosphates (C) triosephosphate isomerase, interconverting DHAP and GAP.
Triosephosphate isomerase rapidly interconverts dihydroxyacetone phosphate with glyceraldehyde 3-phosphate (GADP) that proceeds further into glycolysis. This is advantageous, as it directs dihydroxyacetone phosphate down the same pathway as glyceraldehyde 3-phosphate, simplifying regulation.
The molecule has tertiary folding similar to triosephosphate isomerase and the A-domain of pyruvate kinase, forming an eight strand α/β-barrel structure. [ 3 ] [ 5 ] The α/β-barrel structure is capped on one side by the N-terminal helix.