Pantetheinase

Pantetheinase

Pantetheinase is a ubiquitous enzyme that hydrolyzes D-pantothenic acid to cysteamine and pantothenic acid (vitamin B5) through the dissimilating pathway of coenzyme A[1]. The pantetheinase is encoded by the Vnn (vanin) gene, with Vnn1 being the dominant tissue subtype in both mice and humans[2]. Under physiological conditions, membrane-bound pantetheinase is the main source of cysteamine in tissues. Cysteamine is a potent antioxidant, and Vanin/pantetheinase may be involved in the regulation of certain immune functions. Pantothenic acid is an important component of coenzyme A biosynthesis, and coenzyme A is a crucial cofactor involved in the tricarboxylic acid cycle and fatty acid metabolism. Mercaptoethylamine inhibits glutamylcysteine synthetase, thereby reducing the glutathione pool, which may trigger an inflammatory response. Additionally, functional studies of the enzyme have also shown that pantetheinase is involved in liver lipid metabolism, gluconeogenesis, and inflammation[3].

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