Peptidase M20 domain containing 2 (PM20D2)

Peptidase M20 domain containing 2 (PM20D2) is a metalloenzyme in the metallopeptidase 20 family that acts as a “metabolite repair” enzyme, especially in tissues with active carnosine synthase such as muscle, heart, and brain. Its main role is to hydrolyze noncanonical dipeptides—particularly those derived from β-alanine and γ-aminobutyrate linked to basic amino acids (lysine, ornithine, arginine)—which are produced as byproducts when carnosine synthase uses alternative substrates. PM20D2 thereby prevents their accumulation, ensuring the synthesis of physiologically relevant dipeptides like carnosine and homocarnosine, and contributes to metabolic regulation and dipeptide homeostasis. Human PM20D2 displays 100–200 fold lower enzymatic activity compared to mouse PM20D2[1][4][7].

Other names

BA63L7.3ACY1L2Xaa-Arg dipeptidaseBeta-Ala-Lys dipeptidaseβ-alanyl-lysine dipeptidaseaminoacylase-1-like protein 2xaa-Arg dipeptidaseI(2)-alanyl-lysine dipeptidase