Biotin

Biotin is a vitamin that is a cofactor for enzymes involved in carbon dioxide metabolism. Avidin and streptavidin are proteins that bind biotin very tightly.

Keywords: carboxylase; decarboxylase; transcarboxylase; avidin; streptavidin

Figure 1. Structure of biotin.
Figure 2. Amino acids of streptavidin that bind with biotin.
Figure 3. Schematic illustrating biotin–avidin interactions in the development of biotechnical applications.
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 References
    Athappilly FK and Hendrikson WA (1995) Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing. Structure 3: 1407–1419.
    Chapman-Smith A and Cronan JE (1999) The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity. Trends in Biochemical Sciences 24: 359–363.
    Chapman-Smith A, Turner DL, Cronan JE, Morris TW and Wallace JC (1994) Expression, biotinylation and purification of a biotin-domain peptide from the biotin carboxy carrier protein of Escherichia coli acetyl-CoA carboxylase. Biochemical Journal 302: 881–887.
    Livnah O, Bayer EA, Wilchek M and Sussman JL (1993) Three-dimensional structures of avidin and the avidin–biotin complex. Proceedings of the National Academy of Sciences of the USA 90: 5076–5080.
    Reddy DV, Shenoy BC, Carey PR and Sonnichsen FD (2000) High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii. Biochemistry 39: 2509–2516.
    Roberts EL, Shu N, Howard MJ et al. (1999) Solution structures of apo and holo biotinyl domains from acetyl-coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy. Biochemistry 38: 5045–5053.
    Thoden JB, Blanchard CZ, Holden HM and Waldrop GL (2000) Movement of the biotin carboxylase B-domain as a result of ATP binding. Journal of Biological Chemistry 275: 16183–16190.
    Waldrop GL, Rayment I and Holden HM (1994) Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase. Biochemistry 33: 10249–10256.
    Weber PC, Wendoloski JJ, Pantoliano MW and Salemme FR (1992) Crystallographic and thermodynamic comparison of natural and synthetic ligands bound to streptavidin. Journal of the American Chemical Society 114: 3197–3200.
    book Wilchek M and Bayer EA (eds) (1990) "Avidin–biotin technology". Methods in Enzymology, vol. 184.
    Wilson KP, Shewchuk LM, Brennan RG, Otsuka AJ and Matthews BW (1992) Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proceedings of the National Academy of Sciences of the USA 89: 9257–9261.
 Further Reading
    Artymiuk PJ, Poirrette AR, Rice DW and Willett P (1996) Biotin carboxylase comes into the fold. Nature Structural Biology 3: 128–132.
    Attwood PV (1995) The structure and the mechanism of action of pyruvate carboxylase. International Journal of Biochemistry and Cell Biology 27: 231–249.
    Galperin MY and Koonin EV (1997) A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. Protein Science 6: 2639–2643.
    Jitrapakdee S and Wallace JC (1999) Structure, function and regulation of pyruvate carboxylase. Biochemical Journal 340: 1–16.
    Knowles JR (1989) The mechanism of biotin-dependent enzymes. Annual Review of Biochemistry 58: 195–221.
    Lindqvist Y and Schneider G (1996) Protein–biotin interactions. Current Opinion in Structural Biology 6: 798–803.
    Moss J and Lane MD (1971) The biotin-dependent enzymes. Advances in Enzymology and Related Areas of Molecular Biology 35: 321–442.
    Samols D, Thornton CG, Murtif VL et al. (1988) Evolutionary conservation among biotin enzymes. Journal of Biological Chemistry 263: 6461–6464.
    Toh H, Kondo H and Tanabe T (1993) Molecular evolution of biotin-dependent carboxylases. European Journal of Biochemistry 215: 687–696.
    Wood HG and Barden RE (1977) Biotin enzymes. Annual Review of Biochemistry 46: 385–413.
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How to Cite close
Waldrop, Grover L(May 2002) Biotin. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1038/npg.els.0000644]