The tyrosine aminotransferase from Trypanosoma rangeli: sequence and genomic characterization

The complete sequence and genomic characterization of the tyrosine aminotra nsferase (TAT) gene from Trypanosoma rangeli is reported. The gene was foun d to be organized in a tandem multicopy gene array. A homologous mRNA speci es (2.5 kb) was identified in the epimastigote form of the parasite. From t he deduced amino acid sequence, the gene encodes a protein of 420 amino aci ds 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 cons erved, as well as a pyridoxal-phosphate attachment site typical of class-I aminotransferases. The recombinant enzyme was recognized by a monoclonal an tibody against the T. cruzi enzyme. Additionally, the recombinant protein s howed enzymatic activity when incubated with L-tyrosine and 2-oxoglutaric a cid as substrates. (C) 2000 Federation of European Microbiological Societie s. Published by Elsevier Science B.V. All rights reserved.