The allosteric activator ATP induces a substrate-dependent alteration of the quaternary structure of a mutant aspartate transcarbamoylase impaired in active site closure-Reference-Cited by-同舟云学术

The allosteric activator ATP induces a substrate-dependent alteration of the quaternary structure of a mutant aspartate transcarbamoylase impaired in active site closure

Published:1996-11 Issue:11 Volume:5 Page:2276-2286
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Sci.

Author:

Baker Darren P.,Kantrowitz Evan R.,Vachette Patrice,Fetler Luc

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference39 articles.

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4. Aspartate transcarbamylase: Interaction with the transition state analogue N-(phosphonacetyl)-L-aspartate;Collins;J Biol Chem,1971

5. Function of serine-171 in domain closure, cooperativity and catalysis in Escherichia coli aspartate transcarbamoylase;Dembowski;Biochemistry,1990

Cited by 3 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP onE. coliaspartate transcarbamoylase;Protein Science;2002-05

2. Domain Bridging Interactions;Journal of Biological Chemistry;2001-07

3. Tertiary and quaternary conformational changes in aspartate transcarbamylase: a normal mode study;Proteins: Structure, Function, and Genetics;1999-01-01