Biotin sintaza

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
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PubMed articles
NCBI Protein search

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 ⇌ {\displaystyle \rightleftharpoons } biotin + 2 L-metionin + 2 5'-dezoksiadenozin

Ovaj enzim vezuje [4Fe-4S] i [2Fe-2S] klaster.

Reference

  1. ↑ 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. 
  2. ↑ 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. 
  3. ↑ 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. 
  4. ↑ 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. 
  5. ↑ 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. 
  6. ↑ 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. 
  7. ↑ 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. 
  8. ↑ 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

  • 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. 

Vanjske veze

  • MeSH Biotin+synthase
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TemeTipovi
EC1 Oksidoreduktaze/spisak  • EC2 Transferaze/spisak  • EC3 Hidrolaze/spisak  • EC4 Lijaze/spisak  • EC5 Izomeraze/spisak  • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6