The catalytic mechanism of Escherichia coli aspartate carbamoyltransferase: A molecular modelling study

Eric Gouaux, Kurt L. Krause, William N. Lipscomb

Research output: Contribution to journalArticle

57 Citations (Scopus)

Abstract

Based on a molecular modelling study, we propose that the reaction between L-aspartate and carbamoylphosphate, catalyzed by E. coli aspartate carbamoyltransferase, may proceed via a tetrahedral intermediate and that the breakdown of the intermediate is faciliated by an intramolecular proton transfer between the amino group of L-aspartate and a terminal phosphate oxygen of carbamoylphosphate.

Original languageEnglish (US)
Pages (from-to)893-897
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume142
Issue number3
DOIs
StatePublished - Feb 13 1987
Externally publishedYes

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Aspartate Carbamoyltransferase
Molecular modeling
Aspartic Acid
Escherichia coli
Proton transfer
Protons
Phosphates
Oxygen

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

The catalytic mechanism of Escherichia coli aspartate carbamoyltransferase : A molecular modelling study. / Gouaux, Eric; Krause, Kurt L.; Lipscomb, William N.

In: Biochemical and Biophysical Research Communications, Vol. 142, No. 3, 13.02.1987, p. 893-897.

Research output: Contribution to journalArticle

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