Triose Phosphate Isomerase: Difference between revisions
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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.> | |||
Revision as of 04:14, 20 March 2009
'Triose Phosphate Isomerase
OverviewOverview
(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.
MechanismMechanism
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 CatalysisAcid 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 .<ref name= "web.virginia.edu" [1]>
Structure & FunctionStructure & Function
<Triose Phosphate Isomerase is a dimeric protein of two identical subunits. Each subunit contains 8 alpha helices surrounding 8 interior beta sheets.>
DiseaseDisease
Triose Phosphate Isomerase DeficiencyTriose Phosphate Isomerase Deficiency
See AlsoSee Also
ReferencesReferences
Triose Phosphate Isomerase [[2]] Triose Phosphate Isomerase Deficiency [[3]]