Biotin sintaza
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| Biotin sintaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.8.1.6 | ||||||||
| CAS broj | 80146-93-6 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Biotin sintaza (EC 2.8.1.6, Biotin synthase) je enzim sa sistematskim imenom detiobiotin:sumpor sumportransferaza.[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju
- detiobiotin + [S] + 2 S-adenozil-L-metionin biotin + 2 L-metionin + 2 5'-dezoksiadenozin
Ovaj enzim vezuje [4Fe-4S] i [2Fe-2S] klaster.
Reference[uredi | uredi kod]
- ↑ Trainor, D.A., Parry, R.J. and Gitterman, A. (1980). „Biotin biosynthesis. 2. Stereochemistry of sulfur introduction at C-4 of dethiobiotin”. J. Am. Chem. Soc. 102: 1467-1468.
- ↑ Shiuan, D. and Campbell, A. (1988). „Transcriptional regulation and gene arrangement of Escherichia coli, Citrobacter freundii and Salmonella typhimurium biotin operons”. Gene 67: 203-211. PMID 2971595.
- ↑ Zhang, S., Sanyal, I., Bulboaca, G.H., Rich, A. and Flint, D.H. (1994). „The gene for biotin synthase from Saccharomyces cerevisiae: cloning, sequencing, and complementation of Escherichia coli strains lacking biotin synthase”. Arch. Biochem. Biophys. 309: 29-35. PMID 8117110.
- ↑ Ugulava, N.B., Gibney, B.R. and Jarrett, J.T. (2001). „Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions”. Biochemistry 40: 8343-8351. PMID 11444981.
- ↑ Berkovitch, F., Nicolet, Y., Wan, J.T., Jarrett, J.T. and Drennan, C.L. (2004). „Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme”. Science 303: 76-79. PMID 14704425.
- ↑ Lotierzo, M., Tse Sum Bui, B., Florentin, D., Escalettes, F. and Marquet, A. (2005). „Biotin synthase mechanism: an overview”. Biochem. Soc. Trans. 33: 820-823. PMID 16042606.
- ↑ Taylor, A.M., Farrar, C.E. and Jarrett, J.T. (2008). „9-Mercaptodethiobiotin is formed as a competent catalytic intermediate by Escherichia coli biotin synthase”. Biochemistry 47: 9309-9317. PMID 18690713.
- ↑ Reyda, M.R., Fugate, C.J. and Jarrett, J.T. (2009). „A complex between biotin synthase and the iron-sulfur cluster assembly chaperone HscA that enhances in vivo cluster assembly”. Biochemistry 48: 10782-10792. PMID 19821612.
Literatura[uredi | uredi kod]
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.