Triose Phosphate Isomerase
From Proteopedia
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{{STRUCTURE_1tim | PDB=1tim | SCENE=1}} | {{STRUCTURE_1tim | PDB=1tim | SCENE=1}} | ||
| - | Triose Phosphate Isomerase is a dimeric protein of two identical subunits. Each subunit contains<scene name='Triose_Phosphate_Isomerase/Helices/1'>8 exterior helices</scene> surrounding 8 interior <scene name='Triose_Phosphate_Isomerase/ | + | Triose Phosphate Isomerase is a dimeric protein of two identical subunits. Each subunit contains <scene name='Triose_Phosphate_Isomerase/Helices/1'>8 exterior helices</scene> surrounding 8 interior <scene name='Triose_Phosphate_Isomerase/Beta_sheet/1'>beta sheets</scene> |
Revision as of 01:32, 20 March 2009
'Triose Phosphate Isomerase
Triose Phosphate Isomerase is a dimeric protein of two identical subunits. Each subunit contains surrounding 8 interior
Overview
(TPI or TIM) which catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate, an essential process in the glycolytic pathway.
Mechanism
TPI catalyzes the transfer of a hydrogen atom from carbon 1 to carbon 2, an intramolecular oxidation-reduction. This isomerization of a ketose to an aldose proceeds through an enediol intermediate.<Biochemistry 6th Edition>
Acid Base Catalysis
Glutamate 165 plays the role of the general acid-base catalyst in a proton abstraction mechanism as it abstractluts a proton from carebon 1, which then donates it to carbon 2. Glutamate 165 requires Histidine 95, the general acid
Diagram .[1]
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Gregg Snider, Eric Martz, Michal Harel, Alexander Berchansky, David Canner, Eran Hodis, Stephen Everse, Angel Herraez, Jane S. Richardson
