Enzyme triosephosphate-isomerase

P. Derreumaux and T. Schlick. The loop opening/closing motion of the enzyme triosephosphate isomerase. Biophys. J., 74 72-81, 1998. 

Figure 3 A possible mechanism for the isomerization of dihydroxyacetone phosphate (DHAP) to D glyceraldehyde 3 phosphate (GAP) by the enzyme triosephosphate isomerase (TIM). The general acid (Glu 165) and general base (His 95) are shown.

Figure 2.10 Examples of schematic diagrams of the type pioneered by Jane Richardson. Diagram (a) illustrates the structure of myoglobin in the same orientation as the computer-drawn diagrams of Figures 2.9b-d. Diagram (b), which is adapted from J. Richardson, illustrates the structure of the enzyme triosephosphate isomerase, determined to 2.5 A resolution in the laboratory of David Phillips, Oxford University. Such diagrams can easily be obtained from databases of protein structures, such as PDB, SCOP or CATH, available on the World Wide Web.

Table 4.1 The amino acid residues of the eight parallel p strands in the barrel structure of the enzyme triosephosphate isomerase from chicken muscle...

The enzyme triosephosphate isomerase, abbreviated to TIM, was found to have an important type of structure, now called an a//3 or TIM barrel, consisting of at least 200 residues. In its idealized form, the barrel consists of eight parallel /3 strands connected by eight helixes (Figure 1.19). The strands form the staves of the barrel while the helixes are on the outside and are also parallel (Figure 1.20). (3 strands 1 and 8 are adjacent and form hydrogen bonds with each other. The center of the barrel is a hydrophobic core composed of the side chains of alternate residues of the strands, primarily those of the branched... 

Dihydroxyacetone phosphate is converted to D-glyceraldehyde 3-phosphate by the enzyme triosephosphate isomerase as part of the glycolytic pathway of metabolism. Show how this interconversion could occur by a base-catalyzed mechanism ... 

Step 5 is an isomerization. Dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate are interconverted by the enzyme triosephosphate isomerase. 

Vajda S, Camacho CJ. Protein-protein docking is the glass half-full or half-empty Trends Biotechnol. 2004 22 110-116. Derreumaux P, Schlick T. The loop opening/closing motion of the enzyme triosephosphate isomerase. Biophys. J. 1998 74 72-81. Gerstein M, Chothia C. Analysis of protein loop closure. Two types of hinges produce one motion in lactate dehydrogenase. J. Mol Biol 1991 220 133-149. 

Figure 14.8 Combined glucose and glycerol utilization pathways for 3-HP production. Enzymes triosephosphate isomerase (fpr) GBP dehydrogenase from S. cerevisiae igpdlSc) G-3-phosphatase from S. cerevisiae igpp2Sc) glycerol dehydratase dhaB) alcohol...

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