Carnosine synthase 1 (CARNS1, also known as ATPGD1) catalyses the synthesis of carnosine and homocarnosine, which are abundant dipeptides in skeletal muscle and brain of most vertebrates and some invertebrates [, ].
This is the N-terminal domain found in BL00235 present in Bacillus licheniformis. BL00235 is a ATP-grasp superfamily protein that catalyzes the formation of an alpha-peptide bond between two L-amino acids in an ATP-dependent manner. BL00235 has a highly restricted substrate specificity: the N-terminal substrate is confined to L-methionine an L-leucine, while the C-terminal substrates include small residues such as L-alanine, L-serine, L-threonine and L-cysteine [].This domain can also be found in human CARNS1 (also known as ATPGD1) protein, which catalyzes the synthesis of carnosine and homocarnosine [].
