Carnosine synthase 1 (CARNS1)

Carnosine synthase 1 (CARNS1), also known as ATP-grasp domain-containing protein 3 (ATPGD3), is the primary enzyme responsible for the ATP-dependent synthesis of the dipeptides carnosine (beta-alanyl-L-histidine) and anserine in humans (UniProt Q8N4C0; Drozak et al., 2010). It is predominantly expressed in skeletal muscle and the central nervous system, where these dipeptides serve as critical intracellular pH buffers and antioxidants (Boldyrev et al., 2013). Carnosine also acts as a scavenger of reactive oxygen species and alpha-beta unsaturated aldehydes, providing protection against oxidative stress and glycation (Hipkiss, 2009). Due to these protective roles, CARNS1 is a target of interest for treating neurodegenerative diseases, metabolic disorders like diabetes, and age-related muscle decline. While direct pharmacological activators are not currently in clinical use, the enzyme's pathway is frequently targeted through supplementation with beta-alanine, its rate-limiting substrate, to increase endogenous carnosine levels. Monitoring muscle carnosine content serves as a primary biomarker for the efficacy of such interventions.

Other names

ATP-dependent carnosine synthetase 1ATPGD3ATP-grasp domain-containing protein 3

Catalyzes the ATP-dependent ligation of beta-alanine and L-histidine to form carnosine (beta-alanyl-L-histidine) and anserine.