Abstract: The lysosomal enzyme β-glucocerebrosidase (GCase) belongs to the family of glycosidases and hydrolyses the glycosphingolipid glucosylceramide (GluCer) into glucose and ceramide. The enzyme is of central importance for two pathologies: (1) the lysosomal storage disorder Gaucher’s disease (GD) and (2) the neurodegenerative disorder Parkinson’s disease (PD). GCase is encoded by the gene GBA1 and mutations within GBA1 are the monogenetic cause for GD. This rare lysosomal storage disorder (overall global incidence 0.45–25.0 per 100,000 with high geographical and ethnical variations being more common in the Eastern world and among the Ashkenazi Jewish community with an estimated frequency of 1 in 1000) presents with high heterogeneity (Goker-Alpan and Ivanova, 2024). Due to the accumulation of GluCer, the substrate of GCase, common manifestations include enlarged liver and/or spleen (hepato-/ splenomegaly), anemia, thrombocytopenia as well as skeletal malformations. GD is classified in three types, which are distinguished by the presence and extent of neurological symptoms, including seizures, cognitive impairment, and spasticity (type I: non-neuronopathic; type II: acute neuronopathic; type III: chronic neuronopathic) (Beutler, 2001). Most GD cases (~90%) are related to type I caused by mild GBA1 variants (e.g., N370S). Severe variants (e.g., L444P) are more likely to lead to GD type II or III. All forms of GD are inherited in an autosomal recessive manner. The gold standard for treatment of GD type I is enzyme replacement therapy by regular intravenous administration of recombinant GCase (e.g., Imiglucerase) to overcome peripheral symptoms, such as organomegaly.