Properties of phosphoenolpyruvate mutase, the first enzyme in the aminoethylphosphonate biosynthetic pathway in Trypanosoma cruzi

Sarkar, Mitali, Hamilton, Christopher J. and Fairlamb, Alan H. (2003) Properties of phosphoenolpyruvate mutase, the first enzyme in the aminoethylphosphonate biosynthetic pathway in Trypanosoma cruzi. Journal of Biological Chemistry, 278 (25). pp. 22703-22708. ISSN 0021-9258

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Abstract

Phosphoenolpyruvate ( PEP) mutase catalyzes the conversion of phosphoenolpyruvate to phosphonopyruvate, the initial step in the formation of many naturally occurring phosphonate compounds. The phosphonate compound 2- aminoethylphosphonate is present as a component of complex carbohydrates on the surface membrane of many trypanosomatids including glycosylinositolphospholipids of Trypanosoma cruzi. Using partial sequence information from the T. cruzi genome project we have isolated a full- length gene with significant homology to PEP mutase from the free- living protozoan Tetrahymena pyriformis and the edible mussel Mytilus edulis. Recombinant expression in Escherichia coli confirms that it encodes a functional PEP mutase with a K-m apparent of 8 muM for phosphonopyruvate and a k(cat) of 12 s(-1). The native enzyme is a homotetramer with an absolute requirement for divalent metal ions and displays negative cooperativity for Mg2+ (S-0.5 0.4 muM; n = 0.46). Immunofluorescence and sub- cellular fractionation indicates that PEP mutase has a dual localization in the cell. Further evidence to support this was obtained by Western analysis of a partial sub- cellular fractionation of T. cruzi cells. Southern and Western analysis suggests that PEP mutase is unique to T. cruzi and is not present in the other medically important parasites, Trypanosoma brucei and Leishmania spp.

Item Type:	Article
Uncontrolled Keywords:	phosphate dikinase,pyruvate,phosphonolipids,trypanothione,proteins,tetrahymena-pyriformis,carbon-phosphorus bond,cloning
Faculty \ School:	Faculty of Science > School of Pharmacy
UEA Research Groups:	Faculty of Science > Research Groups > Chemical Biology and Medicinal Chemistry (former - to 2021) Faculty of Science > Research Groups > Medicinal Chemistry (former - to 2017)
Depositing User:	Rachel Smith
Date Deposited:	18 May 2011 09:53
Last Modified:	24 Oct 2022 03:02
URI:	https://ueaeprints.uea.ac.uk/id/eprint/30701
DOI:	10.1074/jbc.M302419200

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