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Yeast Triosephosphate Isomerase, PDB file 1YPI This molecule file is based on the work of E. Lolis, T. Alber, R. C. Davenport, D. Rose, F.C. Hartman, and G.A. Petsko, "Structure of Yeast Triosephosphate Isomerase at 1.9 Angstroms Resolution", Biochemistry, 29, 6609 (1990) and from the Brookhaven PDB file 1YPI. Hydrogen atoms have been added to the original file. |
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Beta barrel motif side view solid ribbons.
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Beta barrel motif side view space fill
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Amino acids critical to the catalytic mechanism, inlcuding lysine 12, histidine 95, glutamate 97, and glutamate 165 are highlighted against the background of the polypeptide backbone. |
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TPI activesite ball and stick. Amino acids critical to the catalytic mechanism, inlcuding lysine 12, histidine 95, glutamate 97, and glutamate 165 are highlighted against the background of the polypeptide backbone. Location of the active site and the specific amino acids involved in the catalysis of the yeast cell triose phosphate isomerase enzyme's substrates. TPI catalyzes the interconversion of glyceraldehyde-3-phosphate and dihydroxyy acetone phosphate in the glycolytic pathway. |
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| TPI active site space filling representation; Amino acids critical to the catalytic mechanism, inlcuding lysine 12, histidine 95, glutamate 97, and glutamate 165 are highlighted against the background of the polypeptide backbone. |
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is a protein. It is not a structural protein. It has
the globular form characteristic of proteins, particularly enzymes, which
influence and regulate functions of cells by catalyzing the tranformation of
biomolecules. TPI is an enzyme which catalyzes the interconversion of
glyceraldehyde-3-phosphate and dihydroxyy acetone phosphate in the glycolytic
pathway.
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 Bacteria |
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