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Originally published In Press as doi:10.1074/jbc.M909220199 on March 19, 2000

J. Biol. Chem., Vol. 275, Issue 21, 15820-15827, May 26, 2000
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Characterization of the Aspartate Transcarbamoylase from Methanococcus jannaschii*

Emily S. HackDagger , Tatyana VorobyovaDagger , Jessica B. Sakash, Jay M. West, Christine P. Macol, Guy Hervé§, Mark K. Williams, and Evan R. Kantrowitz

From the Department of Chemistry, Boston College, Merkert Chemistry Center, Chestnut Hill, Massachusetts 02467 and § Laboratoire de Biochimie des Signaux Régulateurs Cellulaires et Moléculaires, CNRS-UMR 7631, Université Pierre et Marie Curie, 96 Boulevard Raspail, 75006 Paris, France

The genes from the thermophilic archaeabacterium Methanococcus jannaschii that code for the putative catalytic and regulatory chains of aspartate transcarbamoylase were expressed at high levels in Escherichia coli. Only the M. jannaschii PyrB (Mj-PyrB) gene product exhibited catalytic activity. A purification protocol was devised for the Mj-PyrB and M. jannaschii PyrI (Mj-PyrI) gene products. Molecular weight measurements of the Mj-PyrB and Mj-PyrI gene products revealed that the Mj-PyrB gene product is a trimer and the Mj-PyrI gene product is a dimer. Preliminary characterization of the aspartate transcarbamoylase from M. jannaschii cell-free extract revealed that the enzyme has a similar molecular weight to that of the E. coli holoenzyme. Kinetic analysis of the M. jannaschii aspartate transcarbamoylase from the cell-free extract indicates that the enzyme exhibited limited homotropic cooperativity and little if any regulatory properties. The purified Mj-catalytic trimer exhibited hyperbolic kinetics, with an activation energy similar to that observed for the E. coli catalytic trimer. Homology models of the Mj-PyrB and Mj-PyrI gene products were constructed based on the three-dimensional structures of the homologous E. coli proteins. The residues known to be critical for catalysis, regulation, and formation of the quaternary structure from the well characterized E. coli aspartate transcarbamoylase were compared.

* This work was supported by Grant GM26237 from the National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Both authors contributed equally to this work.

To whom correspondence should be addressed. Fax: 617-552-2705; E-mail: evan.kantrowitz@bc.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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