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Carnosinases, their substrates and diseases.

Francesco Bellia¹, Graziella Vecchio², Enrico Rizzarelli³

¹Institute of Biostructure and Bioimaging, CNR, viale A. Doria 6, 95125 Catania, Italy. francesco.bellia@cnr.it.

Molecules (Basel, Switzerland)

|February 26, 2014

Summary

Carnosine dipeptidases, including human carnosinase (CN1 and CN2), hydrolyze key dipeptides. Altered CN1 activity links to diseases, questioning its use as a biomarker.

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Area of Science:

Biochemistry
Enzymology
Molecular Biology

Background:

Carnosinases are Xaa-His dipeptidases with vital roles across all life forms.
Human carnosinase isoforms (CN1 and CN2) hydrolyze dipeptides like carnosine and homocarnosine.
Elevated serum carnosinase (CN1) activity is linked to neurological disorders, chronic diseases, and cancer.

Purpose of the Study:

To review the structure and function of carnosine dipeptidases.
To discuss the physiological and pathological roles of these enzymes.
To describe the primary substrates: carnosine, homocarnosine, and anserine.

Main Methods:

Literature review of carnosinase enzymes.
Analysis of enzyme structure and function.
Examination of substrate hydrolysis and physiological relevance.

Main Results:

Carnosinases (CN1, CN2) and related dipeptidases (PepD, PepV, anserinase) are crucial in imidazole-related dipeptide hydrolysis.
CN1 activity alterations correlate with various pathologies, impacting its utility as a cerebrospinal fluid biomarker.
The review covers enzyme structures, functions, and substrates like carnosine, homocarnosine, and anserine.

Conclusions:

Carnosine dipeptidases are essential enzymes with significant implications in health and disease.
Understanding these enzymes is critical for potential diagnostic and therapeutic applications.
Further research into carnosinase function may elucidate its role in pathological conditions.