The tyrosine aminotransferase from Trypanosoma rangeli: sequence and genomic characterization.
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.
Instituto Nacional de Parasitologia Dr. M. Fatala Chaben, Buenos Aires,Argentina. ejbon@yahoo.com
E J
EJ
Bontempi
G A
GA
García
A
A
Buschiazzo
J
J
Henriksson
C A
CA
Pravia
A M
AM
Ruiz
U
U
Pettersson
V
V
Pszenny
D000595:Amino Acid Sequence; D000818:Animals; D017125:Genes, Protozoan; D016678:Genome; D006801:Humans; D008969:Molecular Sequence Data; D015800:Protozoan Proteins / Q000235:genetics; D051381:Rats; D016415:Sequence Alignment; D017421:Sequence Analysis; D014345:Trypanosoma / Q000201:enzymology* / Q000235:genetics*; D014444:Tyrosine Transaminase / Q000235:genetics*
D015800:Protozoan Proteins; D014444:Tyrosine Transaminase