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The tyrosine aminotransferase from Trypanosoma rangeli: sequence andgenomic characterization
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Genetics and Pathology, Medical Genetics.
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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
Abstract [en]

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.
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Medical Biotechnology
URN: urn:nbn:se:uu:diva-51693DOI: 10.1111/j.1574-6968.2000.tb09239.xPubMedID: 10930747OAI: oai:DiVA.org:uu-51693DiVA: diva2:79602
Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2014-10-28Bibliographically approved

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