Characterization of deoxyuridine 5′‐triphosphate nucleotidohydrolase from Trypanosoma cruzi 1

We report the cloning and kinetic characterization of Trypanosoma cruzi deoxyuridine 5′‐triphosphate nucleotidohydrolase (dUTPase) whose coding sequence was isolated by genetic complementation in Escherichia coli. The deduced amino acid sequence was similar to Leishmania major dUTPase although it ex...

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Bibliographic Details
Published in:FEBS letters 2002-08, Vol.526 (1-3), p.147-150
Main Authors: Bernier-Villamor, Victor, Camacho, Ana, Hidalgo-Zarco, Fernando, Pérez, Juana, Ruiz-Pérez, Luis M, González-Pacanowska, Dolores
Format: Article
Language:English
Subjects:
Chagas’ disease
DMT-dU, 5′-O-(4-4′-dimethoxytrityl)-2′-deoxyuridine
dUDPase
dUTPase
dUTPase, deoxyuridine 5′-triphosphate nucleotidohydrolase
Nucleotide metabolism
Uracil
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Summary:We report the cloning and kinetic characterization of Trypanosoma cruzi deoxyuridine 5′‐triphosphate nucleotidohydrolase (dUTPase) whose coding sequence was isolated by genetic complementation in Escherichia coli. The deduced amino acid sequence was similar to Leishmania major dUTPase although it exhibits an amino acid insertion which is sensitive to protease inactivation. The catalytically active species of the enzyme is a dimer and a detailed kinetic characterization showed that it is highly specific for dUTP and dUDP. The general observation that dUTPases from the Trypanosomatidae differ in sequence, conformation and substrate specificity suggests that a different family of dUTPases exists in certain organisms, which may be exploited as drug targets against infectious diseases.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(02)03158-7