CDP-diacilglicerol—inozitol 3-fosfatidiltransferaza

CDP-diacilglicerol—inozitol 3-fosfatidiltransferaza
CDP-diacilglicerol—inozitol 3-fosfatidiltransferaza homodimer, Mycobacterium tuberculosis
Identifikatori
EC broj 2.7.8.11
CAS broj 2603088
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC articles
PubMed articles
NCBI Protein search

CDP-diacilglicerol—inozitol 3-fosfatidiltransferaza (EC 2.7.8.11, CDP-diglicerid-inozitolna fosfatidiltransferaza, fosfatidilinozitolna sintaza, CDP-diacilglicerol-inozitolna fosfatidiltransferaza, CDP-diglicerid:inozitol transferaza, citidin 5'-difosfo-1,2-diacil-sn-glicerol:mio-inozitol 3-fosfatidiltransferaza, CDP-DG:inozitol transferaza, citidin difosfodiglicerid-inozitolna fosfatidiltransferaza, CDP-diacilglicerol:mio-inozitol-3-fosfatidiltransferaza, CDP-diglicerid-inozitolna transferaza, citidin difosfoglicerid-inozitolna fosfatidiltransferaza, citidin difosfoglicerid-inozitolna transferaza) je enzim sa sistematskim imenom CDP-diacilglicerol:mio-inozitol 3-fosfatidiltransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju

CDP-diacilglicerol + mio-inozitol {\displaystyle \rightleftharpoons } CMP + 1-fosfatidil-1D-mio-inozitol

Reference

  1. Bleasdale, J.E., Wallis, P., MacDonald, P.C. and Johnston, J.M. (1979). „Characterization of the forward and reverse reactions catalyzed by CDP-diacylglycerol:inositol transferase in rabbit lung tissue”. Biochim. Biophys. Acta 575: 135-147. PMID 41587. 
  2. Prottey, C. and Hawthorne, J.N. (1967). „The biosynthesis of phosphatidic acid and phosphatidylinositol in mammalian pancreas”. Biochem. J. 105: 379-392. PMID 4293959. 
  3. Salway, J.G., Harewood, J.L., Kai, M., White, G.L. and Hawthorne, J.N. (1968). „Enzymes of phosphoinositide metabolism during rat brain development”. J. Neurochem. 15: 221-226. PMID 4295616. 
  4. Takenawa, T. and Egawa, K. (1977). „CDP-diglyceride:inositol transferase from rat liver. Purification and properties”. J. Biol. Chem. 252: 5419-5423. PMID 18462. 

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 CDP-diacylglycerol---inositol+3-phosphatidyltransferase
  • p
  • r
  • u
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