Sterol 14-demetilaza

Sterol 14-demetilaza
Identifikatori
EC broj 1.14.13.70
CAS broj 60063-87-8
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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PMC articles
PubMed articles
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Sterol 14-demetilaza (EC 1.14.13.70, obtusufoliolna 14-demetilaza, lanosterolna 14-demetilaza, lanosterolna 14alfa-demetilaza, sterolna 14alfa-demetilaza) je enzim sa sistematskim imenom sterol,NADPH:kiseonik oksidoreduktaza (14-metil odvajanje).[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju

obtusifoliol + 3 O2 + 3 NADPH + 3 H+ ⇌ {\displaystyle \rightleftharpoons } 4alfa-metil-5alfa-ergosta-8,14,24(28)-trien-3beta-ol + format + 3 NADP+ + 4H2O

Ovaj hem-tiolatni enzim (P-450) katalizuje sukcesivne hidroksilacije 14alfa-metil grupe i C-15, čemu sledi eliminacija formata i formiranje 14(15) dvostruke veze.

Reference

  1. ↑ Bak, S., Kahn, R.A., Olsen, C.E. and Halkier, B.A. (1997). „Cloning and expression in Escherichia coli of the obtusifoliol 14α-demethylase of Sorghum bicolor (L.) Moench, a cytochrome P450 orthologous to the sterol 14α-demethylases (CYP51) from fungi and mammals”. Plant J. 11: 191-201. PMID 9076987. 
  2. ↑ Aoyama, Y. and Yoshida, Y. (1991). „Different substrate specificities of lanosterol 14α-demethylase (P450-14DM) of Saccharomyces cerevisiae and rat liver of 24-methylene-24,25-dihydrolanosterol and 24,25-dihydrolanosterol”. Biochem. Biophys. Res. Commun. 178: 1064-1071. PMID 1872829. 
  3. ↑ Aoyama, Y. and Yoshida, Y. (1992). „The 4β-methyl group of substrate does not affect the activity of lanosterol 14α-demethylase (P45014DM) of yeast: differences between the substrate recognition by yeast and plant sterol 14α-demethylases”. Biochem. Biophys. Res. Commun. 183: 1266-1272. PMID 1567403. 
  4. ↑ Alexander, K., Akhtar, M., Boar, R.B., McGhie, J.F. and Barton, D.H.R. (1972). „The removal of the 32-carbon atom as formic acid in cholesterol biosynthesis”. J. Chem. Soc. Chem. Commun.: 383-385. 

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. 

Spoljašnje veze

  • MeSH Sterol+14-demethylase
  • p
  • r
  • u
Proteini: enzimi
Teme
Aktivno mesto  • Alosterna regulacija  • Mesto vezivanja  • Katalitički perfektan enzim  • Koenzim  • Kofaktor  • Kooperativnost  • EC broj  • Enzimska kataliza  • Inhibicija enzima  • Enzimska kinetika  • Lajnviver–Burk dijagram  • Mihaelis–Mentenova kinetika  • Spisak enzima
Tipovi
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