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B6db references: 24817714

type Journal Article
authors Moreno MA, Abramov A, Abendroth J, Alonso A, Zhang S, Alcolea PJ, Edwards T, Lorimer D, Myler PJ, Larraga V.
title Structure of tyrosine aminotransferase from Leishmania infantum
journal Acta Crystallogr F Struct Biol Commun
sel selected
ui 24817714
year (2014)
volume 70
number 5
pages 583-7
keywords Leishmania infantum; tyrosine aminotransferase
abstract The trypanosomatid parasite Leishmania infantum is the causative agent of visceral leishmaniasis (VL), which is usually fatal unless treated. VL has an incidence of 0.5 million cases every year and is an important opportunistic co-infection in HIV/AIDS. Tyrosine aminotransferase (TAT) has an important role in the metabolism of trypanosomatids, catalyzing the first step in the degradation pathway of aromatic amino acids, which are ultimately converted into their corresponding L-2-oxoacids. Unlike the enzyme in Trypanosoma cruzi and mammals, L. infantum TAT (LiTAT) is not able to transaminate ketoglutarate. Here, the structure of LiTAT at 2.35 resolution is reported, and it is confirmed that the presence of two Leishmania-specific residues (Gln55 and Asn58) explains, at least in part, this specific reactivity. The difference in substrate specificity between leishmanial and mammalian TAT and the importance of this enzyme in parasite metabolism suggest that it may be a useful target in the development of new drugs against leishmaniasis.
last changed 2019/05/13 09:56

B6db references