Biotinidinaasin

Biotinidinaasin, also known as biotinidase, is an enzyme that plays a crucial role in the metabolism of biotin, a water-soluble vitamin essential for various biological processes. Biotinidase is found in the mitochondria of eukaryotic cells and is responsible for the hydrolysis of biotin conjugates, which are formed during the synthesis of biotin-containing proteins. This enzyme is particularly important in the degradation of biotin-containing enzymes, such as acetyl-CoA carboxylase and pyruvate carboxylase, which are involved in fatty acid and glucose metabolism, respectively.

The gene encoding biotinidase is located on chromosome 15 in humans. Mutations in this gene can lead to biotinidase deficiency, a rare autosomal recessive disorder characterized by neurological symptoms, including ataxia, seizures, and developmental delays. Individuals with biotinidase deficiency often exhibit elevated levels of biotin-containing enzymes in their blood, which can be used for diagnostic purposes.

Biotinidase is a homodimeric enzyme, consisting of two identical subunits. Each subunit contains a catalytic site that binds biotin conjugates and catalyzes their hydrolysis. The enzyme is highly specific for biotin conjugates and does not hydrolyze free biotin or other biotin analogs. The catalytic mechanism of biotinidase involves the formation of a covalent intermediate between the enzyme and the biotin conjugate, followed by the release of free biotin and the regeneration of the enzyme.

In summary, biotinidase is an enzyme that plays a vital role in the metabolism of biotin, with implications for neurological health and development. Understanding the structure, function, and regulation of biotinidase is essential for the diagnosis and treatment of biotinidase deficiency and other related disorders.