Citrat (Si)-sintaza

Citrat (Si)-sintaza
Citrat sintaza hexamer, Burkholderia thailandensis
Identifikatori
EC broj 2.3.3.1
CAS broj 9027-96-7
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

Citrat (Si)-sintaza (EC 2.3.3.1, (R)-limunska sintaza, citrat kondenzujući enzim, citrat oksaloacetatna lijaza ((pro-3S)-CH2COO-->acetil-KoA), citrat oksaloacetatna lijaza, KoA-acetilacija, citratna sintaza, citratna sintetaza, citrik sintaza, citratni kondenzujući enzim, citrogenaza, kondenzujući enzim, oksaloacetatna transacetaza, oksalacetinska transacetaza) je enzim sa sistematskim imenom acetil-KoA:oksaloacetat C-acetiltransferaza (tioestarska hidroliza, formirane (pro-S)-karboksimetila).[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju

acetil-KoA + H2O + oksaloacetat ⇌ {\displaystyle \rightleftharpoons } citrat + KoA

Stereospecifičnost ovog enzima je suprotna enzimu EC 2.3.3.3, citrat (Re)-sintazi, koji je nađen kod nekoliko anaerobih vrsta.

Reference

  1. ↑ Gottschalk, G. (1969). „Partial purification and some properties of the (R)-citrate synthase from Clostridium acidi-urici”. Eur. J. Biochem. 7: 301-306. PMID 4974734. 
  2. ↑ Ochoa, S., Stern, J.R. and Schneider, M.C. (1951). „Enzymatic synthesis of citric acid. II. Crystalline condensing enzyme”. J. Biol. Chem. 193: 691-702. PMID 14907759. 
  3. ↑ Stern, J.R. (1961). „Oxalacetate transacetase (condensing enzyme, citrogenase)”. u: Boyer, P,D., Lardy, H and Myrbäck, K.. The Enzymes. 5 (2nd izd.). New York: Academic Press. str. 367-380. 
  4. ↑ Rault-Leonardon, M., Atkinson, M.A., Slaughter, C.A., Moomaw, C.R. and Srere, P.A. (1995). „Azotobacter vinelandii citrate synthase”. Biochemistry 34: 257-263. PMID 7819205. 
  5. ↑ Muir, J.M., Russell, R.J., Hough, D.W. and Danson, M.J. (1995). „Citrate synthase from the hyperthermophilic Archaeon, Pyrococcus furiosus”. Prot. Eng. 8: 583-592. PMID 8532683. 
  6. ↑ Russell, R.J., Ferguson, J.M., Hough, D.W., Danson, M.J. and Taylor, G.L. (1997). „The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9 Å resolution”. Biochemistry 36: 9983-9994. PMID 9254593. 

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. 
  • Stern, J.R. (1961). „Oxalacetate transacetase (condensing enzyme, citrogenase)”. u: Boyer, P,D., Lardy, H and Myrbäck, K.. The Enzymes. 5 (2nd izd.). New York: Academic Press. str. 367-380. 

Spoljašnje veze

  • MeSH Citrate+(Si)-synthase
  • 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