Focusing on the functional characterization of the anserinase from Oreochromis niloticus(64 visite) Pirone L, Di Gaetano S, Rizzarelli E, Bellia F, Pedone E
Int J Biol Macromol (ISSN: 0141-8130linking, 1879-0003electronic), 2019 Feb 22; 130: 158-165.
Tipo di articolo: Journal Article,
Impact factor: 4.784, Impact factor a 5 anni: 3.227
Url: Non disponibile.
Parole chiave: Anserine, Dipeptidases, Transition Metal Ions,
*** IBB - CNR *** Institute of Biostructure and Bioimaging, CNR, Napoli, Italy., Institute of Biostructure and Bioimaging, CNR, Catania, Italy; Department of Chemical Sciences, University of Catania, Catania, Italy., Institute of Biostructure and Bioimaging, CNR, Catania, Italy. Electronic address: firstname.lastname@example.org., Institute of Biostructure and Bioimaging, CNR, Napoli, Italy. Electronic address: email@example.com.,
Carnosine, anserine and homocarnosine are the three most representative compounds of the histidine dipeptides family, widely distributed in mammals in different amounts depending on the species and the tissue considered. Histidine dipeptides are mainly degraded by two different carnosinase homologues: a highly specific metal-ion dependent carnosinase (CN1) located in serum and brain and a non-specific cytosolic form (CN2). The hydrolysis of such dipeptides in prokaryotes and eukaryotes is also catalyzed by the anserinase (ANSN). Such naturally occurring dipeptides represent an interesting topic because they seem to have numerous biological roles such as potential neuroprotective and neurotransmitter functions in the brain and therefore ANSN results to be a very interesting target of study. We here report, for the first time, cloning, expression of ANSN from the fish Oreochromis niloticus both in a mammalian and in a prokaryotic system, in order to perform deep functional studies by enzymatic assays in the presence of different metals and substrates. Furthermore, by means of a mass spectrometry-based proteomic approach, we analysed protein sequence and the potential presence of post-translational modifications in the mammalian recombinant protein. Finally, a preliminary structural characterization was carried out on ANSN produced in Escherichia coli.