JBC Advanced Glycation Endproducts

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Originally published In Press as doi:10.1074/jbc.M208185200 on September 19, 2002

J. Biol. Chem., Vol. 277, Issue 47, 45466-45472, November 22, 2002
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Unmasking a Functional Allosteric Domain in an Allosterically Nonresponsive Carbamoyl-phosphate Synthetase*

Binnur Eroglu and Susan G. Powers-LeeDagger

From the Department of Biology, Northeastern University, Boston, Massachusetts 02115

Although carbamoyl-phosphate synthetases (CPSs) share sequence identity, multidomain structure, and reaction mechanism, they have varying physiological roles and allosteric effectors. Escherichia coli CPS (eCPS) provides CP for both arginine and pyrimidine nucleotide biosynthesis and is allosterically regulated by metabolites from both pathways, with inhibition by UMP and activation by IMP and ornithine. The arginine-specific CPS from Saccharomyces cerevisiae (sCPS), however, apparently responds to no allosteric effectors. We have designed and analyzed a chimeric CPS (chCPS, in which the C-terminal 136 residues of eCPS were replaced by the corresponding residues of sCPS) to define the structural basis for the allosteric nonresponsiveness of sCPS and thereby provide insight into the mechanism for allosteric selectivity and responsiveness in the other CPSs. Surprisingly, ornithine and UMP each had a significant effect on chCPS activity, and did so at concentrations that were similar to those effective for eCPS. We further found that sCPS bound both UMP and IMP and that chCPS bound IMP, although none of these interactions led to changes in enzymatic activity. These findings strongly suggest that the nonresponsive sCPS is not able to communicate occupancy of the allosteric site to the active site but does contain a latent allosteric interaction domain.

* This work was supported by National Institutes of Health Grant DK54423.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 To whom correspondence should be addressed. Tel.: 617-373-2385; Fax: 617-373-3724; E-mail: spl@neu.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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