The tyrosine aminotransferase from Trypanosoma rangeli: sequence andgenomic characterization
2000 (English)In: FEMS Microbiology Letters, ISSN 0378-1097, E-ISSN 1574-6968, Vol. 189, no 2, 253-257 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2000. Vol. 189, no 2, 253-257 p.
IdentifiersURN: urn:nbn:se:uu:diva-51693DOI: 10.1111/j.1574-6968.2000.tb09239.xPubMedID: 10930747OAI: oai:DiVA.org:uu-51693DiVA: diva2:79602