Triose Phosphate Isomerase
From Proteopedia
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| - | <scene name='Triose_Phosphate_Isomerase/Helices/1'>8 exterior helices</scene> | ||
== Overview == | == Overview == | ||
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== Structure & Function == | == Structure & Function == | ||
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| + | Triose Phosphate Isomerase is a dimeric protein of two identical subunits. Each subunit contains 8 alpha helices<scene name='Triose_Phosphate_Isomerase/Helices/1'>8 exterior helices</scene> surrounding 8 interior beta sheets. | ||
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== Disease == | == Disease == | ||
Revision as of 01:10, 20 March 2009
'Triose Phosphate Isomerase
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]
Proteopedia Page Contributors and Editors (what is this?)
Gregg Snider, Eric Martz, Michal Harel, Alexander Berchansky, David Canner, Eran Hodis, Stephen Everse, Angel Herraez, Jane S. Richardson
