Catalytic efficiency of designed catalytic proteins

Ivan V. Korendovych, William F. DeGrado

Research output: Contribution to journalReview article

60 Scopus citations

Abstract

The de novo design of catalysts that mimic the affinity and specificity of natural enzymes remains one of the Holy Grails of chemistry. Despite decades of concerted effort we are still unable to design catalysts as efficient as enzymes. Here we critically evaluate approaches to (re)design of novel catalytic function in proteins using two test cases: Kemp elimination and ester hydrolysis. We show that the degree of success thus far has been modest when the rate enhancements seen for the designed proteins are compared with the rate enhancements by small molecule catalysts in solvents with properties similar to the active site. Nevertheless, there are reasons for optimism: the design methods are ever improving and the resulting catalyst can be efficiently improved using directed evolution.

Original languageEnglish (US)
Pages (from-to)113-121
Number of pages9
JournalCurrent Opinion in Structural Biology
Volume27
Issue number1
DOIs
StatePublished - Aug 2014

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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