Triosephosphate isomerase (TPI or TIM) is a functionally and structurally well-known enzyme that play a crucial role in glycolytic and gluconeogenic metabolism. TPI interconverts dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (G3P) [1]
Structure and Function
of some thermophilic sepecies exist as a homotetramer due to the hard physiological environment, however, it exists as a dimer in solution [2]. Each subunits of homotetramer forms TIM barrel in which 8α helices alternate with 8β sheets to form backbone of the protein. Hydrophobic chain form the core enzyme whereas hydrophilic found near the ends of the barrel where exposed to solvent. Each subunit has it own active site and only active as a dimer . The on chain A includes Gly 70, His 71, Asp 61, Leu 94, Arg 92, and His 59
Disease
Relevance
Structural highlights
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