Molecules 2014, 19(2), 2299-2329; doi:10.3390/molecules19022299
Review

Carnosinases, Their Substrates and Diseases

1 Institute of Biostructure and Bioimaging, CNR, viale A. Doria 6, 95125 Catania, Italy 2 Department of Chemical Sciences, University of Catania, viale A. Doria 6, 95125 Catania, Italy
* Author to whom correspondence should be addressed.
Received: 25 October 2013; in revised form: 7 January 2014 / Accepted: 28 January 2014 / Published: 21 February 2014
(This article belongs to the Special Issue Enzyme Chemistry)
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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 (β-alanyl-L-histidine) and homocarnosine (γ-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 imidazole-related 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 (β-alanyl-3-methyl-L-histidine) will also be described.
Keywords: carnosine; carnosinase; dipeptide; metallopeptidase; biomarker

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MDPI and ACS Style

Bellia, F.; Vecchio, G.; Rizzarelli, E. Carnosinases, Their Substrates and Diseases. Molecules 2014, 19, 2299-2329.

AMA Style

Bellia F, Vecchio G, Rizzarelli E. Carnosinases, Their Substrates and Diseases. Molecules. 2014; 19(2):2299-2329.

Chicago/Turabian Style

Bellia, Francesco; Vecchio, Graziella; Rizzarelli, Enrico. 2014. "Carnosinases, Their Substrates and Diseases." Molecules 19, no. 2: 2299-2329.

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