Abstract

The simplest chemical transformations in metabolism are the proton transfer reactions exemplified by certain isomerases and racemases. We have been studying three such enzymes to understand the structural features that lead to efficient proton transfer. All of these enzymes face the common problem of abstracting a hydrogen from a carbon acid of high pKa with an enzymic base of low pKa. We have used X-ray crystallography, site-directed mutagenesis, and molecular dynamics simulations to arrive at a set of principles for optimal catalysis of this simple reaction.

Keywords

IsomeraseChemistryProtonMutagenesisCatalysisEnzymeActive siteEnzyme catalysisMolecular dynamicsStereochemistryComputational chemistryBiochemistryMutationPhysics

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Year
1993
Type
article
Citations
43
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Gregory A. Petsko, Dagmar Ringe, Karen N. Allen et al. (1993). The structural enzymology of proton-transfer reactions. Protein Engineering Design and Selection . https://doi.org/10.1093/protein/6.supplement.37-a

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DOI
10.1093/protein/6.supplement.37-a