Please use this identifier to cite or link to this item: http://sgc.anlis.gob.ar/handle/123456789/495
Title: The tyrosine aminotransferase from Trypanosoma rangeli: sequence and genomic characterization
Authors: Bontempi, Esteban 
Garcia, G. A. 
Buschiazzo, A. 
Henriksson, J. 
Pravia, Carlos 
Ruiz, Andrés Mariano 
Pettersson, Ulf 
Pszenny, Viviana 
Issue Date: 2000
Description: The complete sequence and genomic characterization of the tyrosine aminotransferase (TAT) gene from Trypanosoma rangeli is reported. The gene was found to be organized in a tandem multicopy gene array. A homologous mRNA species (2.5 kb) was identified in the epimastigote form of the parasite. From the deduced amino acid sequence, the gene encodes a protein of 420 amino acids with a predicted molecular mass of 46.4 kDa and a theoretical pI of 6.23. A high sequence identity was found with the Trypanosoma cruzi, human and rat enzymes. All the essential residues for TAT enzymatic activity are conserved, as well as a pyridoxal-phosphate attachment site typical of class-I aminotransferases. The recombinant enzyme was recognized by a monoclonal antibody against the T. cruzi enzyme. Additionally, the recombinant protein showed enzymatic activity when incubated with L-tyrosine and 2-oxoglutaric acid as substrates. (C) 2000 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
URI: http://sgc.anlis.gob.ar/handle/123456789/495
Rights: restrictedAccess
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