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Characterization of deoxyuridine 5′‐triphosphate nucleotidohydrolase from Trypanosoma cruzi 1
Author(s) -
Bernier-Villamor Victor,
Camacho Ana,
Hidalgo-Zarco Fernando,
Pérez Juana,
Ruiz-Pérez Luis M,
González-Pacanowska Dolores
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03158-7
Subject(s) - biochemistry , peptide sequence , escherichia coli , complementation , biology , protein fragment complementation assay , deoxyuridine , enzyme , chemistry , microbiology and biotechnology , dna , gene , mutant
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.