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Carnosinases, Their Substrates and Diseases

Authors :: Graziella Vecchio
Francesco Bellia
Enrico Rizzarelli
Source :: Molecules (Basel, Online) 19 (2014): 2299–2329. doi:10.3390/molecules19022299, info:cnr-pdr/source/autori:Bellia, Francesco; Vecchio, Graziella; Rizzarelli, Enrico/titolo:Carnosinases, their substrates and diseases/doi:10.3390%2Fmolecules19022299/rivista:Molecules (Basel, Online)/anno:2014/pagina_da:2299/pagina_a:2329/intervallo_pagine:2299–2329/volume:19, Molecules, Vol 19, Iss 2, Pp 2299-2329 (2014), Molecules
Publication Year :: 2014
Publisher :: MDPI AG, 2014.
Abstract: Carnosinases are Xaa-His dipeptidases that play diverse functions throughout all kingdoms of life. Human isoforms of carnosinase (CN1 and CN2) under appropriate conditions catalyze the hydrolysis of the dipeptides carnosine (?-alanyl-L-histidine) and homocarnosine (?-aminobutyryl-L- histidine). Alterations of serum carnosinase (CN1) activity has been associated with several pathological conditions, such as neurological disorders, chronic diseases and cancer. For this reason the use of carnosinase levels as a biomarker in cerebrospinal fluid (CSF) has been questioned. The hydrolysis of imidazolerelated dipeptides in prokaryotes and eukaryotes is also catalyzed by aminoacyl-histidine dipeptidases like PepD (EC 3.4.13.3), PepV (EC 3.4.13.19) and anserinase (EC 3.4.13.5). The review deals with the structure and function of this class of enzymes in physiological and pathological conditions. The main substrates of these enzymes, i.e., carnosine, homocarnosine and anserine (?-alanyl-3-methyl-L-histidine) will also be described. © 2014 by the authors; licensee MDPI, Basel, Switzerland.