1987•Cold Spring Harbor Symposia on Quantitative BiologyRequires access
Crystallography and Site-directed Mutagenesis of Yeast Triosephosphate Isomerase: What Can We Learn about Catalysis from a "Simple" Enzyme?
Tom Alber, R. Davenport, Debra Ann Giammona, Elias Lolis, Gregory A. Petsko, Dagmar Ringe
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Abstract
If there is any hope of completely understanding the catalytic action of any enzyme, surely the best candi-date for the protein is triosephosphate isomerase (TIM). (Following a convention initially established by Knowles's and Phillips's groups at Oxford, we use TIM as an abbreviation for the enzyme and TPI to represent its gene.) This enzyme catalyzes the simplest reaction in all of metabolic biochemistry, the interconversion of the 3-carbon triosephosphates dihydroxyacetone phos-phate (DHAP) and o-glyceraldehyde-3-phosphate (o-GAP). The reaction is just the transfer of a proton, the pro-R hydrogen from carbon 1 of DHAP, stereospecifi-cally to carbon 2 to form the o-isomer of GAP (Fig. 1). Isomerization of these two sugar phosphates, which are the products of the aldolase-catalyzed degradation of