SDSL encodes a pyridoxal-phosphate-dependent enzyme that catalyzes the dehydrative deamination of L-serine and L-threonine, producing ammonia and pyruvate or alpha-ketobutyrate respectively. The protein also exhibits racemase activity toward glutamate. SDSL localizes to the cytosol and participates in amino acid catabolism. In a mouse model of ulcerative colitis, SDSL gene expression was regulated as part of a broader metabolic response to disease, with changes in SDSL expression correlating with alterations in amino acid metabolism 1. Recent multiomic studies identified SDSL among signature genes associated with dilated cardiomyopathy, where its expression correlated with immune cell infiltration and cuproptosis-related pathways 2. SDSL is implicated in multiple disease contexts including 12q14 microdeletion syndrome and other skeletal and developmental disorders listed in disease databases, though the specific mechanistic contributions to these phenotypes remain to be fully characterized. The gene represents a potential diagnostic biomarker for cardiomyopathy-associated pathology, though targeted therapeutic strategies have not yet been established.