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Review
. 2009 Jan-Feb;35(1):36-46.
doi: 10.1002/biof.8.

Biotin

Affiliations
Review

Biotin

Janos Zempleni et al. Biofactors. 2009 Jan-Feb.

Abstract

Biotin is a water-soluble vitamin and serves as a coenzyme for five carboxylases in humans. Biotin is also covalently attached to distinct lysine residues in histones, affecting chromatin structure and mediating gene regulation. This review describes mammalian biotin metabolism, biotin analysis, markers of biotin status, and biological functions of biotin. Proteins such as holocarboxylase synthetase, biotinidase, and the biotin transporters SMVT and MCT1 play crucial roles in biotin homeostasis, and these roles are reviewed here. Possible effects of inadequate biotin intake, drug interactions, and inborn errors of metabolism are discussed, including putative effects on birth defects.

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Figures

Fig. 1
Fig. 1
Pathways of biotin catabolism.
Fig. 2
Fig. 2
Biotin-dependent carboxylases. ACC, acetyl-CoA carboxylase; MCC, 3-methylcrotonyl-CoA carboxylase; PC, pyruvate carboxylase; PCC, propionyl-CoA carboxylase.
Fig. 3
Fig. 3
The structure of chromatin. [Color figure can be viewed in the online issue, which is available at www.interscience.wiley.com.]
Fig. 4
Fig. 4
Modification sites in histories H2A, H3, and H4. Ac, acetate; B, biotin; M, methyl; P, phosphate; U, ubiquitin, [Color figure can be viewed in the online issue, which is available at www.interscience.wiley.com.]

References

    1. Boas MA. The effect of desiccation upon the nutritive properties of egg-white. Biochem. J. 1927;21:712–724. - PMC - PubMed
    1. Kogl F, Tonnis B. Über das Bios-Problem. Darstellung von krystallisiertem Biotin aus Eigelb. Z. Physiol Chem. 1932;242:43–73.
    1. du Vigneaud V, Melville DB, Folkers K, Wolf DE, Mozingo DE, Keresztesy JC, Harris SA. The structure of biotin: a study of desthiobiotin. J. Biol. Chem. 1942;146:475–485.
    1. Harris SA, Wolf DE, Mozingo R, Folkers K. Synthetic biotin. Science. 1943;97:447–448. - PubMed
    1. Hatakeyama K, Kobayashi M, Yukawa H. Analysis of biotin biosynthesis pathway in coryneform bacteria: Brevibacterium flavum. In: McCormick DB, Suttie JW, Wagner C, editors. Vitamins and Coenzymes, Part I. San Diego, CA: Academic Press; 1997. pp. 339–348. - PubMed

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