Abstract
Proton (H+) transfers play a central role in many enzymatic reactions.1 A good illustration is provided by serine protease reactions.2–4 In a recent theoretical study4 of the serine protease tripsin-catalyzed hydrolysis of a specific tripeptide substrate, there are no less than four proton transfer steps, beginning with a serine to histidine H+ transfer in the Michaelis complex (Fig. 1) Another example is furnished in a study5, 6 of the reversible isomerization of dihydroxyacetone (DHAP) to glyceraldehyde 3-phosphate (GAP) by the enzyme triose phosphate isomerase (TIM). A key step in the DHAP ⇌ GAP reaction is the proton abstraction by a carboxylate group in Glu 165 of a CH proton in DHAP (Fig. 2).
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Borgis, D., Hynes, J.T. (1989). Proton Transfer Reactions. In: Cooper, A., Houben, J.L., Chien, L.C. (eds) The Enzyme Catalysis Process. Progress in Mathematics. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-1607-8_20
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DOI: https://doi.org/10.1007/978-1-4757-1607-8_20
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