Carboxypeptidase Taq -like peptidases from Trypanosomatids

NIEMIROWICZ, GABRIELA TERESA; FRASCH, ALEJANDRA PAULA; CAZZULO, JUAN JOSÉ

Handbook of Proteolytic Enzymes, 3rd Edition

ELSEVIER

Año: 2013; p. 1253 - 1257

Among eukaryotic organisms, the M32 family of peptidases seems to be restricted to a very limited number of phylogenetic groups, including the family Trypanosomatidae (a family containing several parasites of medical and veterinary importance) and some unicellular algae. Trypanosoma cruzi metallocarboxypeptidase-1 (TcMCP-1), an enzyme present in the causative agent of the American Trypanosomiasis, Chagas Disease, was the first eukaryotic M32 peptidase to be characterized in both sequence and structure [1, 2]. Unlike previously characterized prokaryotic M32 MCPs [3, 4], this new family member was characterized by the presence of a paralog gene, TcMCP-2. This second enzyme, present exclusively in T. cruzi (no orthologous sequences were found in other trypanosomatids) was found to complement TcMCP-1 substrate specicity. A third M32 carboxypeptidase, LmaCP1, was described in Leishmania major [5]. This enzyme, restricted to the Leishmania genus, presented a different substrate specicity compared to TcMCPs.