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Microbiology and Molecular Biology Reviews, September 2001, p. 404-421, Vol. 65, No. 3
1092-2172/01/$04.00+0   DOI: 10.1128/MMBR.65.3.404-421.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Allosteric Regulation of Catalytic Activity: Escherichia coli Aspartate Transcarbamoylase versus Yeast Chorismate Mutase

Kerstin Helmstaedt, Sven Krappmann, and Gerhard H. Braus*

Abteilung Molekulare Mikrobiologie, Institut für Mikrobiologie und Genetik, Georg-August-Universität, Göttingen, Germany

Allosteric regulation of key metabolic enzymes is a fascinating field to study the structure-function relationship of induced conformational changes of proteins. In this review we compare the principles of allosteric transitions of the complex classical model aspartate transcarbamoylase (ATCase) from Escherichia coli, consisting of 12 polypeptides, and the less complicated chorismate mutase derived from baker's yeast, which functions as a homodimer. Chorismate mutase presumably represents the minimal oligomerization state of a cooperative enzyme which still can be either activated or inhibited by different heterotropic effectors. Detailed knowledge of the number of possible quaternary states and a description of molecular triggers for conformational changes of model enzymes such as ATCase and chorismate mutase shed more and more light on allostery as an important regulatory mechanism of any living cell. The comparison of wild-type and engineered mutant enzymes reveals that current textbook models for regulation do not cover the entire picture needed to describe the function of these enzymes in detail.

* Corresponding author. Mailing address: Abteilung Molekulare Mikrobiologie, Institut für Mikrobiologie und Genetik, Georg-August-Universität, Grisebachstr. 8, D-37077 Göttingen, Germany. Phone: (49) 551-393771. Fax: (49) 551-393820. E-mail: gbraus{at}gwdg.de.

Microbiology and Molecular Biology Reviews, September 2001, p. 404-421, Vol. 65, No. 3
1092-2172/01/$04.00+0   DOI: 10.1128/MMBR.65.3.404-421.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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