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
Grover L Waldrop, Louisiana State University, Baton Rouge, Louisiana, USA
Published online: May 2002
DOI: 10.1038/npg.els.0000644
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
| References | |
| Athappilly FK and Hendrikson WA (1995) Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing. Structure 3: 14071419. | |
| Chapman-Smith A and Cronan JE (1999) The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity. Trends in Biochemical Sciences 24: 359363. | |
| 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: 881887. | |
| Livnah O, Bayer EA, Wilchek M and Sussman JL (1993) Three-dimensional structures of avidin and the avidinbiotin complex. Proceedings of the National Academy of Sciences of the USA 90: 50765080. | |
| 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: 25092516. | |
| 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: 50455053. | |
| 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: 1618316190. | |
| Waldrop GL, Rayment I and Holden HM (1994) Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase. Biochemistry 33: 1024910256. | |
| 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: 31973200. | |
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| Further Reading | |
| Artymiuk PJ, Poirrette AR, Rice DW and Willett P (1996) Biotin carboxylase comes into the fold. Nature Structural Biology 3: 128132. | |
| Attwood PV (1995) The structure and the mechanism of action of pyruvate carboxylase. International Journal of Biochemistry and Cell Biology 27: 231249. | |
| Galperin MY and Koonin EV (1997) A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. Protein Science 6: 26392643. | |
| Jitrapakdee S and Wallace JC (1999) Structure, function and regulation of pyruvate carboxylase. Biochemical Journal 340: 116. | |
| Knowles JR (1989) The mechanism of biotin-dependent enzymes. Annual Review of Biochemistry 58: 195221. | |
| Lindqvist Y and Schneider G (1996) Proteinbiotin interactions. Current Opinion in Structural Biology 6: 798803. | |
| Moss J and Lane MD (1971) The biotin-dependent enzymes. Advances in Enzymology and Related Areas of Molecular Biology 35: 321442. | |
| Samols D, Thornton CG, Murtif VL et al. (1988) Evolutionary conservation among biotin enzymes. Journal of Biological Chemistry 263: 64616464. | |
| Toh H, Kondo H and Tanabe T (1993) Molecular evolution of biotin-dependent carboxylases. European Journal of Biochemistry 215: 687696. | |
| Wood HG and Barden RE (1977) Biotin enzymes. Annual Review of Biochemistry 46: 385413. | |