SYNTHESIS OF GALACTOSE ANALOGS

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The question of how enzymes utilize binding interactions directed to nonreacting parts of substrate molecules to catalyze the chemical transformations of the reacting parts of substrates is one principalfocus of my research. These interactions provide the energy for thestructural transition of enzymes into active conformations. Statementsthat are commonly advanced to explain enzymatic catalysis by theactive conformation of an enzyme include those in which the enzyme ispostulated to stabilize transition states or to destabilize groundstates in enzyme-substrate complexes, or both. These are very generalstatements that do not explicitly account for the actions ofparticular enzymes. A specific description of catalysis, in bothstructural and dynamic terms, is needed for a few enzymes. Serineproteases, isomerases, and the enzymes of galactose metabolism aresubjects of my research in this field.