Open AccessThe tyrosine aminotransferase from Trypanosoma rangeli : sequence and genomic characterization
Author(s) -
Bontempi Esteban J.,
García Gabriela A.,
Buschiazzo Alejandro,
Henriksson Jan,
Pravia Carlos A.,
Ruiz Andrés M.,
Pettersson Ulf,
Pszenny Viviana
Publication year - 2000
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2000.tb09239.x
Subject(s) - biology , biochemistry , peptide sequence , gene , recombinant dna , trypanosoma cruzi , microbiology and biotechnology , tyrosine aminotransferase , enzyme , molecular cloning , amino acid , tyrosine , sequence analysis , parasite hosting , enzyme inducer , world wide web , computer science
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 p I 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.