The structural enzymology of proton-transfer reactions

Gregory Petsko, Dagmar Ringe, Karen Allen, Arnon Lavie, Eva Gerhart-Mueller, James Clifton, Miriam Hasson, Shigeo Fujita, Shigetoshi Sugio, Xidhong Xhang, Robert Davenport, Elias Lolis, David Neidhart, George Kenyon, John Gerlt, Paul Bash, Jeremy Knowles, Martin Karplus

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish (US)
Pages (from-to)37
Number of pages1
JournalProtein Engineering, Design and Selection
StatePublished - 1993
Externally publishedYes

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Molecular Biology


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