Literature DB >> 3548720

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

J E Gouaux, K L Krause, W N Lipscomb.   

Abstract

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

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Year:  1987        PMID： 3548720     DOI： 10.1016/0006-291x(87)91497-5

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  15 in total

Review 1.  Substrate-assisted catalysis: molecular basis and biological significance.

Authors:  W Dall'Acqua; P Carter
Journal:  Protein Sci       Date:  2000-01       Impact factor: 6.725

Review 2.  Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase.

Authors:  K Helmstaedt; S Krappmann; G H Braus
Journal:  Microbiol Mol Biol Rev       Date:  2001-09       Impact factor: 11.056

3.  The α-amino group of the threonine substrate as the general base during tRNA aminoacylation: a new version of substrate-assisted catalysis predicted by hybrid DFT.

Authors:  Wenjuan Huang; Eric A C Bushnell; Christopher S Francklyn; James W Gauld
Journal:  J Phys Chem A       Date:  2011-09-26       Impact factor: 2.781

4.  A molecular mechanism for pyrimidine and purine nucleotide control of aspartate transcarbamoylase.

Authors:  R C Stevens; W N Lipscomb
Journal:  Proc Natl Acad Sci U S A       Date:  1992-06-15       Impact factor: 11.205

Review 5.  Structure and mechanisms of Escherichia coli aspartate transcarbamoylase.

Authors:  William N Lipscomb; Evan R Kantrowitz
Journal:  Acc Chem Res       Date:  2011-10-19       Impact factor: 22.384

6.  Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase.

Authors:  J E Gouaux; W N Lipscomb
Journal:  Proc Natl Acad Sci U S A       Date:  1988-06       Impact factor: 11.205

7.  Crystallographic snapshots of the complete catalytic cycle of the unregulated aspartate transcarbamoylase from Bacillus subtilis.

Authors:  Katharine M Harris; Gregory M Cockrell; David E Puleo; Evan R Kantrowitz
Journal:  J Mol Biol       Date:  2011-05-31       Impact factor: 5.469

8.  The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativity.

Authors:  C Macol; M Dutta; B Stec; H Tsuruta; E R Kantrowitz
Journal:  Protein Sci       Date:  1999-06       Impact factor: 6.725

9.  Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: characterization of the active site and evidence for an interdomain carboxy-terminal helix in ornithine transcarbamoylase.

Authors:  L B Murata; H K Schachman
Journal:  Protein Sci       Date:  1996-04       Impact factor: 6.725

10.  Submicromolar phosphinic inhibitors of Escherichia coli aspartate transcarbamoylase.

Authors:  Laëtitia Coudray; Evan R Kantrowitz; Jean-Luc Montchamp
Journal:  Bioorg Med Chem Lett       Date:  2008-12-06       Impact factor: 2.823
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