CNDP2 (carnosine dipeptidase 2) is a metallodipeptidase that catalyzes the formation of bioactive metabolites with significant roles in energy homeostasis and cellular signaling. The enzyme's primary function involves conjugating lactate with amino acids to produce N-lactoyl-amino acids, particularly N-lactoyl-phenylalanine (Lac-Phe), which acts as an exercise-inducible metabolite that suppresses feeding and reduces obesity 1. CNDP2 also catalyzes the conjugation of β-hydroxybutyrate with amino acids, generating BHB-amino acids that similarly regulate energy balance during ketosis 2. Mechanistically, CNDP2 is expressed in diverse cell types including macrophages, monocytes, immune cells, and intestinal epithelial cells, where it mediates metabolite biosynthesis through enzymatic conjugation reactions 13. The enzyme plays a critical role in tumor biology by enabling cooperative nutrient scavenging through extracellular oligopeptide hydrolysis, supporting cancer cell survival in nutrient-deprived environments 4. Additionally, CNDP2-generated Lac-Phe exhibits anti-inflammatory properties by inhibiting M1 macrophage polarization via NF-κB pathway suppression 5. In ovarian cancer, CNDP2 promotes tumorigenesis and metastasis through PI3K/AKT pathway activation 6. These findings establish CNDP2 as a key metabolic regulator linking physical activity, energy balance, inflammation, and cancer progression.