Triose Phosphate Isomerase Structure & Mechanism
From Proteopedia
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| - | Triose phosphate isomerase (TIM)<ref>PMID:16511037</ref> (PDB [[1wyi]]) is a crucial enzyme in the glycolytic pathway. <scene name='Christian_Krenk_Sandbox/Nc_rainbow/1'>TIM</scene> reversibly converts the aldose Glyceraldehyde-3-phosphate ( | + | Triose phosphate isomerase (TIM)<ref>PMID:16511037</ref> (PDB [[1wyi]]) is a crucial enzyme in the glycolytic pathway. <scene name='Christian_Krenk_Sandbox/Nc_rainbow/1'>TIM</scene> reversibly converts the aldose Glyceraldehyde-3-phosphate (GAP) to the ketose Dihydroxyacetone phosphate (DHAP). The interconversion proceeds by an enediol intermediate. |
==Structural Characteristics of TIM== | ==Structural Characteristics of TIM== | ||
| - | The secondary structure consists of 14 alpha helices and 8 beta sheets per monomer, making it fall in the SCOP category of alpha and beta proteins. <scene name='Christian_Krenk_Sandbox/Alpha_beta_barrel/2'> | + | The secondary structure consists of 14 alpha helices and 8 beta sheets per monomer, making it fall in the SCOP category of alpha and beta proteins. The tertiary structure is a <scene name='Christian_Krenk_Sandbox/Alpha_beta_barrel/2'>alpha-beta barrel.</scene> |
The quaternary structure is a homodimer. | The quaternary structure is a homodimer. | ||
Revision as of 20:18, 1 March 2010
Contents |
Triose Phosphate Isomerase (TIM)
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Triose phosphate isomerase (TIM)[1] (PDB 1wyi) is a crucial enzyme in the glycolytic pathway. reversibly converts the aldose Glyceraldehyde-3-phosphate (GAP) to the ketose Dihydroxyacetone phosphate (DHAP). The interconversion proceeds by an enediol intermediate.
Structural Characteristics of TIM
The secondary structure consists of 14 alpha helices and 8 beta sheets per monomer, making it fall in the SCOP category of alpha and beta proteins. The tertiary structure is a The quaternary structure is a homodimer.
Mechanism of TIM
The enzyme aids in catalysis by binding tightly to the enediol transition state. To convert GAP to the enediol intermediate, a proton is abstracted from C2 by a base and the carbonyl oxygen atom is protonated by an acid. To convert the enediol intermediate to DHAP, C1 is protonated by Glu 165, with His 95 removing a proton from C2’s OH group. As a result, the catalytic groups are back at their original states, and catalysis is completed.
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| 1wyi, resolution 2.20Å () | |||||||||
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| Activity: | Triose-phosphate isomerase, with EC number 5.3.1.1 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
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| 1hti, resolution 2.80Å () | |||||||||
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| Ligands: | |||||||||
| Activity: | Triose-phosphate isomerase, with EC number 5.3.1.1 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
References
- ↑ Kinoshita T, Maruki R, Warizaya M, Nakajima H, Nishimura S. Structure of a high-resolution crystal form of human triosephosphate isomerase: improvement of crystals using the gel-tube method. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Apr 1;61(Pt, 4):346-9. Epub 2005 Mar 24. PMID:16511037 doi:10.1107/S1744309105008341
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Christian Krenk, Alexander Berchansky, Diamond B. Reese, Michal Harel, Jane S. Richardson, David Canner
