Triose Phosphate Isomerase
From Proteopedia
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[[Image:TPI mechanism.jpg]] | [[Image:TPI mechanism.jpg]] | ||
| - | Diagram .<ref name= "web.virginia.edu" [http://web.virginia.edu/Heidi/chapter19/Images/8883n19_15.jpg] | + | Diagram .<ref name= "web.virginia.edu" [http://web.virginia.edu/Heidi/chapter19/Images/8883n19_15.jpg]> |
== Structure & Function == | == Structure & Function == | ||
Revision as of 00:52, 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
