Literature DB >> 4561937

Conformational changes in aspartate trancarbamylase. I. Studies of ligand binding and of subunit interactions by circular dichroism spectroscopy.

J H Griffin, J P Rosenbusch, K K Weber, E R Blout.   

Abstract

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Year:  1972        PMID： 4561937

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


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  8 in total

Review 1.  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

2.  Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase.

Authors:  Jie Wang; Kimberly A Stieglitz; James P Cardia; Evan R Kantrowitz
Journal:  Proc Natl Acad Sci U S A       Date:  2005-06-10       Impact factor: 11.205

3.  Aspartate transcarbamylase from the deep-sea hyperthermophilic archaeon Pyrococcus abyssi: genetic organization, structure, and expression in Escherichia coli.

Authors:  C Purcarea; G Hervé; M M Ladjimi; R Cunin
Journal:  J Bacteriol       Date:  1997-07       Impact factor: 3.490

4.  ATP binding to a protease-resistant core of actin.

Authors:  G R Jacobson; J P Rosenbusch
Journal:  Proc Natl Acad Sci U S A       Date:  1976-08       Impact factor: 11.205

5.  Importance of the loop at residues 230-245 in the allosteric interactions of Escherichia coli aspartate carbamoyltransferase.

Authors:  S A Middleton; E R Kantrowitz
Journal:  Proc Natl Acad Sci U S A       Date:  1986-08       Impact factor: 11.205

6.  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

7.  A single amino acid substitution in the active site of Escherichia coli aspartate transcarbamoylase prevents the allosteric transition.

Authors:  Kimberly A Stieglitz; Styliani C Pastra-Landis; Jiarong Xia; Hiro Tsuruta; Evan R Kantrowitz
Journal:  J Mol Biol       Date:  2005-04-09       Impact factor: 5.469

8.  Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, NMR, and X-ray crystallographic study.

Authors:  J W Stebbins; D E Robertson; M F Roberts; R C Stevens; W N Lipscomb; E R Kantrowitz
Journal:  Protein Sci       Date:  1992-11       Impact factor: 6.725
  8 in total

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