pantothenate kinase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: ATP + pantothenate = ADP + D-4'-phosphopantothenate. [EC:2.7.1.33]

Pantothenate kinase activity is a crucial step in the biosynthesis of coenzyme A (CoA), a ubiquitous cofactor essential for numerous metabolic pathways. CoA plays a critical role in various cellular processes, including carbohydrate, lipid, and amino acid metabolism, as well as the regulation of gene expression. Pantothenate kinases catalyze the phosphorylation of pantothenate (vitamin B5), the precursor to CoA, utilizing ATP as the phosphate donor. The reaction results in the formation of 4'-phosphopantothenate, which is further metabolized to CoA. Pantothenate kinases are highly conserved enzymes found in all living organisms. They exhibit a high degree of specificity for pantothenate, ensuring the efficient and selective production of CoA. The active site of these enzymes typically contains a conserved motif known as the "pantothenate kinase motif," which is involved in binding pantothenate and ATP. The catalytic mechanism involves the transfer of a phosphate group from ATP to the hydroxyl group at the 4' position of pantothenate. This phosphorylation step is essential for the subsequent steps in CoA biosynthesis. In addition to their role in CoA biosynthesis, pantothenate kinases have been implicated in other cellular processes, including cell growth, proliferation, and inflammation. Dysregulation of pantothenate kinase activity has been linked to various diseases, including cancer and neurodegenerative disorders. Therefore, pantothenate kinases are attractive targets for drug development, particularly for the treatment of diseases related to CoA metabolism.'
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Proteins (1)

Compounds (2)