Triose Phosphate Isomerase
From Proteopedia
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These two catalytic residues include <scene name='Triose_Phosphate_Isomerase/Glu_165/1'>Glutamate 165</scene> which plays the role of the general base catalyst in a proton abstraction mechanism as it abstracts a proton from carbon 1, which then donates it to carbon 2. Glutamate 165 requires <scene name='Triose_Phosphate_Isomerase/His95/2'>Histidine 95</scene>, the general acid which donates a proton to the C-1 carbonyl oxygen. | These two catalytic residues include <scene name='Triose_Phosphate_Isomerase/Glu_165/1'>Glutamate 165</scene> which plays the role of the general base catalyst in a proton abstraction mechanism as it abstracts a proton from carbon 1, which then donates it to carbon 2. Glutamate 165 requires <scene name='Triose_Phosphate_Isomerase/His95/2'>Histidine 95</scene>, the general acid which donates a proton to the C-1 carbonyl oxygen. | ||
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| - | Diagram .<ref name= "web.virginia.edu" [http://web.virginia.edu/Heidi/chapter19/Images/8883n19_15.jpg]> | ||
== Structure & Function == | == Structure & Function == | ||
Revision as of 15:29, 21 March 2009
Triose Phosphate Isomerase is a dimeric protein of two identical subunits. Each subunit contains surrounding 8 interior
Contents |
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
TPI carries out the isomerization reaction through acid base chemistry involving
These two catalytic residues include which plays the role of the general base catalyst in a proton abstraction mechanism as it abstracts a proton from carbon 1, which then donates it to carbon 2. Glutamate 165 requires , the general acid which donates a proton to the C-1 carbonyl oxygen.
Structure & Function
Triose Phosphate Isomerase is a dimeric protein of two identical subunits. Each subunit contains 8 alpha helices surrounding 8 interior beta sheets.
Disease
Triose Phosphate Isomerase Deficiency
See Also
References
Triose Phosphate Isomerase [[1]] Triose Phosphate Isomerase Deficiency [[2]]
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
