thiamine binding

Definition

Target type: molecularfunction

Binding to thiamine (vitamin B1), a water soluble vitamin present in fresh vegetables and meats, especially liver. [GOC:mlg]

Thiamine binding is a crucial molecular function involving the interaction of thiamine (vitamin B1) with specific proteins, primarily enzymes, to facilitate a variety of metabolic processes. Thiamine, a water-soluble vitamin, is essential for the proper function of several key enzymes, including pyruvate dehydrogenase complex (PDC), α-ketoglutarate dehydrogenase complex (KGDHC), and transketolase, which play vital roles in carbohydrate metabolism. The binding of thiamine to these enzymes occurs through a specific structural motif called the thiamine pyrophosphate (TPP) binding site. This site is typically located in the active site of the enzyme and is composed of a series of amino acid residues that interact with the TPP molecule. The interaction between TPP and the enzyme is crucial for the catalytic activity of the enzyme. TPP acts as a cofactor, enabling the enzyme to catalyze the transfer of a carboxyl group from a keto acid to a substrate. This transfer reaction is essential for the breakdown of carbohydrates and the production of energy in the form of ATP. Specifically, TPP is involved in the decarboxylation of α-keto acids, a key step in carbohydrate metabolism. The binding of thiamine to these enzymes is highly specific, ensuring that the proper cofactor is used for each enzymatic reaction. Thiamine deficiency can lead to various metabolic disorders, including beriberi, a disease characterized by neurological and cardiovascular symptoms. The understanding of thiamine binding at the molecular level has been instrumental in elucidating the mechanisms of carbohydrate metabolism and the development of therapies for thiamine deficiency diseases.'
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Proteins (1)

Compounds (1)