Transition state variation in enzymatic reactions

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Abstract

Experimental analysis of enzymatic transition states by kinetic isotope effect methods has established geometric variation in related transition state structures. Differences are apparent in development of the reaction coordinate, in solvolytic transition states relative to those in enzymatic catalytic sites, in the stereochemistry of related substrates at the transition state, and in reactions catalyzed by related enzymes.

Original languageEnglish (US)
Pages (from-to)556-563
Number of pages8
JournalCurrent Opinion in Chemical Biology
Volume5
Issue number5
DOIs
StatePublished - Oct 1 2001

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Stereochemistry
Isotopes
Catalytic Domain
Kinetics
Substrates
Enzymes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Transition state variation in enzymatic reactions. / Schramm, Vern L.

In: Current Opinion in Chemical Biology, Vol. 5, No. 5, 01.10.2001, p. 556-563.

Research output: Contribution to journalArticle

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