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J. Biol. Chem., Vol. 281, Issue 41, 30717-30724, October 13, 2006

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Dichotomic Phylogenetic Tree of the Pyruvate Kinase Family

K⁺-DEPENDENT AND -INDEPENDENT ENZYMES^*

From the Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, 04510 México, D. F., México

K⁺ dependence was assumed to be a feature of all pyruvate kinases until it was discovered that some enzymes express K⁺ -independent activity. Almost all the K⁺-independent pyruvate kinases have Lys at position 117, instead of the Glu present in the K⁺-dependent muscle enzyme. Mutagenesis studies show that the internal positive charge substitutes for the K⁺ requirement (Laughlin, L. T. & Reed, G. H. (1997) Arch. Biochem. Biophys. 348, 262–267). In this work a phylogenetic analysis of pyruvate kinase was performed to ascertain the abundance of K⁺ -independent activities and to explore whether the K⁺ activating effect is related to the evolutionary history of the enzyme. Of the 230 studied sequences, 46% have Lys at position 117, and the rest have Glu. Pyruvate kinases with Lys¹¹⁷ and Glu¹¹⁷ are separated in two clusters. All of the enzymes of the Glu¹¹⁷ cluster that have been characterized are K⁺-dependent, whereas those of the Lys¹¹⁷ cluster are K⁺-independent. Thus, there is a strict correlation between the dichotomy of the tree and the dependence of activity on K⁺. 77% of the pyruvate kinases that possess Lys¹¹⁷ have Lys¹¹³/Gln¹¹⁴; they also have Ile, Val, or Leu at position 120. These residues are replaced by Glu¹¹⁷ and Thr¹¹³/Lys¹¹⁴/Thr¹²⁰ in 80% of K⁺-dependent pyruvate kinases. Structural analysis indicates that these residues are in a hinge region involved in the acquisition of the catalytic conformation of the enzyme. The route of conversion from K⁺-independent to K⁺-dependent pyruvate kinases is described. A plausible explanation of how enzymes developed K⁺ dependence is put forth.

Received for publication, June 2, 2006 , and in revised form, August 9, 2006.

^* This work was supported by Grant IN202906 (to L. R.-S.) from the Dirección General de Asuntos del Personal Académico de la Universidad Nacional Autónoma de México (DGAPA-UNAM), México. 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Appendix 1.

¹ To whom correspondence should be addressed: Departamento de Bioquímica, Facultad de Medicina, Apartado Postal 70-159, Universidad Nacional Autónoma de México, 04510, D. F., México. Tel.: 525-6232510; Fax: 525-6162419; E-mail: lramirez{at}bq.unam.mx.

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