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Figure 6
(a) Left, an overview of the structure of triosephosphate isomerase from S. cerevisiae (PDB entry 1ney; Jogl et al., 2003BB40) 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. (2010BB96) and Richard (2012BB69).

IUCrJ
Volume 4| Part 1| January 2017| Pages 50-64
ISSN: 2052-2525
https://doi.org/10.1107/S2052252516018017
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