Citrat (Si)-sintaza
Citrat (Si)-sintaza | |||||||||
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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 | ||||||||
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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 citrat + KoA
Stereospecifičnost ovog enzima je suprotna enzimu EC 2.3.3.3, citrat (Re)-sintazi, koji je nađen kod nekoliko anaerobih vrsta.
Reference
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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
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
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