Abstract
Carnosine (β-alanyl-L-histidine) and its methylated derivatives: anserine (β-alanyl-Nπ- methyl-L-histidine) and balenine (β-alanyl-Nτ-methyl-L-histidine) are abundant constituents of excitable tissues of vertebrates. While carnosine and anserine are present at high concentrations and in variable proportions in skeletal muscle and brain of most vertebrates, balenine appears to be rather more abundant in marine mammals and certain reptilian species. Since the discovery of these compounds at the beginning of 20th century, numerous studies have been devoted to identification of the biochemical and physiological properties of carnosine and related dipeptides. These led to the discovery of the pHbuffering, metal-chelation and antioxidant, capabilities of carnosine and anserine, although no definitive ideas concerning their physiological role has yet been formulated. Only recently the molecular identities of the enzymes catalyzing synthesis of carnosine (carnosine synthase, EC 6.3.2.11) and anserine (carnosine N-methyltransferase, EC 2.1.1.22) have been elucidated, which has given a new insight into their metabolism in vertebrates. These findings have opened new research areas and provide authentic opportunities for understanding the biological function of these “enigmatic” dipeptides. This review aims to summarize recent advances in our knowledge concerning enzymes responsible for the biosynthesis of carnosine and related dipeptides and to evaluate their importance in vertebrate physiology.
Keywords: Anserine, balenine, biosynthesis, carnosine, carnosine synthase, carnosine N-methyltransferase, CARNS1, CARNMT1, HNMT-like, homocarnosine, UPF0586.
Graphical Abstract
Related Journals
Protein & Peptide Letters
Related Books
Frontiers in Protein and Peptide Sciences
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