Molecular orbital studies of reaction mechanism and transition state structures for GABA-transaminase

Peter R. Andrews, Magdy Iskander, Graham Jones, David A. Winkler

Research output: Contribution to journalArticleOther

6 Citations (Scopus)

Abstract

The reaction catalyzed by the enzyme GABA-transaminase has been studied by means of semi-empirical molecular orbital calculations. The results elucidate the role of the active site general base and the cofactor in reducing the barrier to a 1,3-prototropic shift, the rate-determining step in the transamination reaction. The mechanistic inferences drawn are consistent with previous studies of pyridoxal phosphate-dependent transaminases. 

Original languageEnglish
Pages (from-to)125-132
Number of pages8
JournalEuropean Journal of Medicinal Chemistry
Volume23
Issue number2
DOIs
Publication statusPublished - 1988

Keywords

  • enzyme inhibitors
  • GABA-transaminase
  • molecular orbital study
  • pyridoxal phosphate
  • reaction mechanism
  • transition state

Cite this

Andrews, Peter R. ; Iskander, Magdy ; Jones, Graham ; Winkler, David A. / Molecular orbital studies of reaction mechanism and transition state structures for GABA-transaminase. In: European Journal of Medicinal Chemistry. 1988 ; Vol. 23, No. 2. pp. 125-132.
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Molecular orbital studies of reaction mechanism and transition state structures for GABA-transaminase. / Andrews, Peter R.; Iskander, Magdy; Jones, Graham; Winkler, David A.

In: European Journal of Medicinal Chemistry, Vol. 23, No. 2, 1988, p. 125-132.

Research output: Contribution to journalArticleOther

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AU - Iskander, Magdy

AU - Jones, Graham

AU - Winkler, David A.

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