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J. Biol. Chem., Vol. 280, Issue 18, 18321-18325, May 6, 2005

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From ATP as Substrate to ADP as Coenzyme

FUNCTIONAL EVOLUTION OF THE NUCLEOTIDE BINDING SUBUNIT OF DIHYDROXYACETONE KINASES^*

Christoph Bächler, Karin Flükiger-Brühwiler, Philipp Schneider, Priska Bähler, and Bernhard Erni

From the Departement für Chemie und Biochemie, Universität Bern, Freiestrasse 3, CH-3012 Bern, Switzerland

Dihydroxyacetone kinases are a family of sequence-related enzymes that utilize either ATP or a protein of the phosphoenolpyruvate:sugar phosphotransferase system (PTS) as a source of high energy phosphate. The PTS is a multicomponent system involved in carbohydrate uptake and control of carbon metabolism in bacteria. Phylogenetic analysis suggests that the PTS-dependent dihydroxyacetone kinases evolved from an ATP-dependent ancestor. Their nucleotide binding subunit, an eight-helix barrel of regular up-down topology, retains ADP as phosphorylation site for the double displacement of phosphate from a phospho-histidine of the PTS protein to dihydroxyacetone. ADP is bound essentially irreversibly with a t of 100 min. Complexation with ADP increases the thermal unfolding temperature of dihydroxyacetone L from 40 (apo-form) to 65 °C (holoenzyme). ADP assumes the same role as histidines, cysteines, and aspartic acids in histidine kinases and PTS proteins. This conversion of a substrate binding site into a cofactor binding site reflects a remarkable instance of parsimonious evolution.

Received for publication, January 10, 2005 , and in revised form, February 18, 2005.

^* This work was supported by Swiss National Science Foundation Grant 3100A0-105247. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 41-31-6314346; Fax: 41-31-6314887; E-mail: erni{at}ibc.unibe.ch.

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