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Journal of Bacteriology, December 1998, p. 6389-6391, Vol. 180, No. 23
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Aspartate Transcarbamylase from the Hyperthermophilic Eubacterium Thermotoga maritima: Fused Catalytic and Regulatory Polypeptides Form an Allosteric Enzyme

Pingguo Chen,1,2 Françoise Van Vliet,3 Mark Van De Casteele,1,2,dagger Christianne Legrain,3 Raymond Cunin,1,2 and Nicolas Glansdorff1,2,3,*

Laboratory for Genetics and Microbiology, Vrije Universiteit Brussel,1 Department of Microbiology, Flanders Interuniversity Institute for Biotechnology,2 and Jean-Marie Wiame Institute for Microbiological Research,3 Brussels, Belgium

Received 19 June 1998/Accepted 21 September 1998

In the allosteric aspartate transcarbamylase (ATCase) from the hyperthermophilic eubacterium Thermotoga maritima, the catalytic and regulatory functions, which in class B ATCases are carried out by specialized polypeptides, are combined on a single type of polypeptide assembled in trimers. The ATCases from T. maritima and Treponema denticola present intriguing similarities, suggesting horizontal gene transfer.

* Corresponding author. Mailing address: Dept. of Microbiology, Flanders Interuniversity Institute for Biotechnology, E. Gryson Ave., 1070 Brussels, Belgium. Phone: 32-2-526 72 75. Fax: 32-2-526 72 73. E-mail: ceriair{at}ulb.ac.be.

dagger Present address: Laboratory for Metabolism and Endocrinology, Vrije Universiteit Brussel, 1090 Brussels, Belgium.

Journal of Bacteriology, December 1998, p. 6389-6391, Vol. 180, No. 23
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

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