Interplay of organic and biological chemistry in understanding coenzyme mechanisms: Example of thiamin diphosphate-dependent decarboxylations of 2-oxo acids

Frank Jordan

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

With the publication of the three-dimensional structures of several thiamin diphosphate-dependent enzymes, the chemical mechanism of their non-oxidative and oxidative decarboxylation reactions is better understood. Chemical models for these reactions serve a useful purpose to help evaluate the additional catalytic rate acceleration provided by the protein component. The ability to generate, and spectroscopically observe, the two key zwitterionic intermediates invoked in such reactions allowed progress to be made in elucidating the rates and mechanisms of the elementary steps leading to and from these intermediates. The need remains to develop chemical models, which accurately reflect the enzyme-bound conformation of this coenzyme. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)298-301
Number of pages4
JournalFEBS Letters
Volume457
Issue number3
DOIs
StatePublished - Sep 3 1999

All Science Journal Classification (ASJC) codes

  • Genetics
  • Molecular Biology
  • Biophysics
  • Structural Biology
  • Biochemistry
  • Cell Biology

Keywords

  • 2-Oxo acid decarboxylase
  • Enzyme model
  • Thiamin diphosphate
  • Zwitterionic intermediate

Fingerprint Dive into the research topics of 'Interplay of organic and biological chemistry in understanding coenzyme mechanisms: Example of thiamin diphosphate-dependent decarboxylations of 2-oxo acids'. Together they form a unique fingerprint.

Cite this