Triose Phosphate Isomerase

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[[image:TPI2.png]]
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{{STRUCTURE_1tim | PDB=1tim | SCENE=}}
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{{STRUCTURE_1tim | PDB=1tim | SCENE=1}}
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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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== 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.
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 01:22, 20 March 2009

'Triose Phosphate Isomerase

Image:TPI2.png

Template:STRUCTURE 1tim

Triose Phosphate Isomerase is a dimeric protein of two identical subunits. Each subunit contains 8 alpha helices surrounding 8 interior beta sheets.


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

Image:TPI mechanism.jpg

Diagram .[1]

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