Structural and kinetic studies of Schistosoma mansoni adenylate kinases

Ivo De Almeida Marques, Larissa Romanello, Ricardo DeMarco, Humberto D Muniz Pereira

Research output: Contribution to journalArticlepeer-review

Abstract

The human parasite Schistosoma mansoni is totally dependent on the purine salvage pathway in order to supply large quantities of purine precursors for its energy and DNA biosynthetic needs. Adenylate kinase (ADK) is responsible for the conversion of AMP (produced by the adenosine kinase reaction) into ADP, which is subsequently converted into ATP by nucleoside diphosphate kinase (NDPK). ADK and NDPK are the most active enzymes of the pathway, probably reflecting an evolutionary adaptation due to the intense use of the branch in which they participate. However, notwithstanding their importance very little information has been accumulated found regarding these enzymes. In this work two adenylate kinases from S. mansoni were cloned and heterologously expressed in Escherichia coli. The purified products were utilized in activity assays, and displayed kinetic parameters similar to the corresponding human orthologous proteins. The cytosolic S. mansoni ADK was crystallized and its structure solved allowing us to detect a difference in the nucleotide binding site when compared with the human ortholog.

Original languageEnglish (US)
Pages (from-to)157-160
Number of pages4
JournalMolecular and Biochemical Parasitology
Volume185
Issue number2
DOIs
StatePublished - Oct 2012
Externally publishedYes

Keywords

  • Adenylate kinase
  • Crystal structure
  • Kinetics
  • Purine salvage pathway
  • Schistosoma mansoni

ASJC Scopus subject areas

  • Molecular Biology
  • Parasitology

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