of carnitine is unnecessary for active site binding, but vital for the catalysis to proceed. This has been proven to be the case through the synthesis of a carnitine analog lacking its trimethylammonium group. This compound was able to compete with carnitine in binding to CRAT, but was unable to induce a reaction. The emergence of subtrate-assisted catalysis has opened up new strategies for increasing synthetic substrate specificity. Biological function There is evidence that suggests that CRAT activity is necessary for the cell cycle to proceed from the G1 phase to the S phase. Clinical significance Those with an inherited deficiency in CRAT activity are at risk for developing severe heart and neurological problems. Reduced CRAT activity can be found in individuals suffering from Alzheimer’s disease. CRAT and its family of enzymes have great potential as targets for developing therapeutic treatments for Type 2 diabetes and other diseases. Interactions CRAT is known to interact with NEDD8, PEX5, SUMO1. References Further reading AgRP Neurons Require Carnitine Acetyltransferase to Regulate Metabolic Flexibility and Peripheral Nutrient Partitioning ] EC 2.3.1 Enzymes of known structure