biotinidase deficiency/histone

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Biotinylation of histones by human serum biotinidase: assessment of biotinyl-transferase activity in sera from normal individuals and children with biotinidase deficiency.

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Serum biotinidase has biotinyl-transferase activity in addition to biocytin hydrolase activity. A sensitive assay for biotinyl-transferase activity was developed based on the transfer of biotin from biocytin to histones. Biotinidase biotinyl-transferase occurs at physiological and alkaline pHs,

Drosophila melanogaster holocarboxylase synthetase is a chromosomal protein required for normal histone biotinylation, gene transcription patterns, lifespan, and heat tolerance.

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Post-translational modifications of histones play important roles in chromatin structure and genomic stability. Distinct lysine residues in histones are targets for covalent binding of biotin, catalyzed by holocarboxylase synthetase (HCS) and biotinidase (BTD). Histone biotinylation has been

Biotinidase: its role in biotinidase deficiency and biotin metabolism.

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Renewed interest in biotinidase, the enzyme responsible for recycling the vitamin biotin, initially came from the discovery of biotinidase deficiency in 1982. Since then, the elucidation of other activities of the enzyme, alternative splicing of the biotinidase gene and differential subcellular

Biotin and biotinidase deficiency.

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Biotin is a water-soluble vitamin that serves as an essential coenzyme for five carboxylases in mammals. Biotin-dependent carboxylases catalyze the fixation of bicarbonate in organic acids and play crucial roles in the metabolism of fatty acids, amino acids and glucose. Carboxylase activities

Biotinidase and its roles in biotin metabolism.

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Biotinidase is the enzyme responsible for the recycling of the vitamin biotin. Biotinidase acts as a hydrolase by cleaving biocytin and biotinyl-peptides, thereby liberating biotin for reutilization. Biotinidase is also important for making biotin bioavailable from bound dietary sources. The

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