CADEE: Computer-Aided Directed Evolution of Enzymes

Amrein, B.A.; Steffen-Munsberg, F.; Szeler, I.; Purg, M.; Kulkarni, Y.; Kamerlin, S.C.L.

doi:10.1107/S2052252516018017

Figure 6
(a) Left, an overview of the structure of triosephosphate isomerase from S. cerevisiae (PDB entry 1ney; Jogl et al., 2003

) in complex with DHAP (displayed in ball-and-stick representation and coloured dark grey). Right, a close-up view of the active site, with highlighted key catalytic residues His95 and Glu165 and the substrate DHAP. Chain A is coloured green and chain B light grey. (b) The proposed mechanism for the isomerization catalysed by TIM. DHAP and GAP are acronyms for dihydroxyacetone phosphate and (R)-glyceraldehyde 3-phosphate, respectively. This mechanism is based on Wierenga et al. (2010