Barth syndrome is a complicated and life-threatening systemic disease. It is characterized by a wide range of conditions, mostly affecting the heart and skeletal muscles. Symptoms include cardiomyopathy, skeletal myopathy, neutropenia, increased urinary excretion of 3-methylglutaconic acid and weaker motor skills. Being a genetic disease, it is currently uncurable and is managed through medications that decrease symptom severity. The syndrome is caused by mutations in the TAZ gene which encodes the tafazzin enzyme. Tafazzin has an important role in the cardiolipin synthesis and remodeling pathway. Cardiolipin is a unique phospholipid that makes up a significant portion of the inner mitochondrial membrane. It goes through a complex and highly conserved synthesis and remodeling pathway which is altered in patients with Barth syndrome. Unlike other phospholipids, cardiolipin has a specific structure that differs from other phospholipids and enables it to interact with various membrane proteins and complexes, playing a crucial role in maintaining mitochondrial energy metabolism. By gaining a deeper understanding of the molecular mechanisms and the significance of cardiolipin synthesis and remodeling, new treatment strategies could be developed. These strategies would target the underlying cause of the disease, unlike currently available therapeutic approaches. One potential target is beta-oxidation. Trimetazidine, a drug commonly used to treat heart conditions, inhibits beta-oxidation and has been shown in previous studies to affect mitochondrial phospholipid turnover. However, its impact on cardiolipin synthesis and turnover remains unknown. In this research, we are interested in investigating if inhibition of beta-oxidation enhances mitochondrial phospholipid turnover and increases the levels of functional cardiolipin in cells with TAZ deficiencies. Saccharomyces cerevisiae serves as an excellent model organism for studying Barth syndrome because all the enzymatic steps involved in cardiolipin synthesis and remodeling are conserved between yeast and humans.