The role of cysteine 206 in allosteric inhibition of Escherichia coli citrate synthase. Studies by chemical modification, site-directed mutagenesis, and 19F NMR.-Reference-Cited by-同舟云学术

The role of cysteine 206 in allosteric inhibition of Escherichia coli citrate synthase. Studies by chemical modification, site-directed mutagenesis, and 19F NMR.

Published:1991-11 Issue:31 Volume:266 Page:20709-20713
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Donald L.J.,Crane B.R.,Anderson D.H.,Duckworth H.W.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference22 articles.

1. In vitro mutagenesis of Escherichia coli citrate synthase to clarify the locations of ligand binding sites.

2. Mutation of amino acids thought to polarize the oxaloacetate carbonyl in citrate synthase severely reduces but does not abolish activity of the enzyme

3. Amino acid sequence of Escherichia coli citrate synthase

4. The kinetics of enzyme-catalyzed reactions with two or more substrates or products

5. Functional groups in the activity and regulation of Escherichia coli citrate synthase

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