1-Acilglicerofosfoholin O-aciltransferaza
1-Acilglicerofosfoholin O-aciltransferaza | |||||||||
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Identifikatori | |||||||||
EC broj | 2.3.1.23 | ||||||||
CAS broj | 9027-64-9 | ||||||||
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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1-Acilglicerofosfoholin O-aciltransferaza (EC 2.3.1.23, lizolecitinska aciltransferaza, 1-acil-sn-glicero-3-fosfoholinska aciltransferaza, acil koenzim A-monoacilfosfatidilholinska aciltransferaza, acil-KoA:1-acil-glicero-3-fosfoholinska transacilaza, lizofosfatidna aciltransferaza, lizofosfatidilholinska aciltransferaza) je enzim sa sistematskim imenom acil-KoA:1-acil-sn-glicero-3-fosfoholin O-aciltransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- acil-KoA + 1-acil-sn-glicero-3-fosfoholin KoA + 1,2-diacil-sn-glicero-3-fosfoholin
Ovaj enzim preferentno deluje na nezasićene acil-KoA derivate. 1-acil-sn-glicero-3-fosfoinozitol takođe mođe da bude akceptor.
Reference
- ↑ Bell, R.M. and Coleman, R.A. (1980). „Enzymes of glycerolipid synthesis in eukaryotes”. Annu. Rev. Biochem. 49: 459-487. PMID 6250446.
- ↑ Hill, E.E. and Lands, W.E.M. (1968). „Incorporation of long-chain and polyunsaturated acids into phosphatidate and phosphatidylcholine”. Biochim. Biophys. Acta 152: 645-648. PMID 5661029.
- ↑ Miki, Y., Hosaka, K., Yamashita, S., Handa, H. and Numa, S. (1977). „Acyl-acceptor specificities of 1-acylglycerolphosphate acyltransferase and 1-acylglycerophosphorylcholine acyltransferase resolved from rat liver microsomes”. Eur. J. Biochem. 81: 433-441. PMID 598375.
- ↑ van den Bosch, H., van Golde, L.M.G., Eibl, H. and van Deenen, L.L.M. (1967). „The acylation of 1-acylglycero-3-phosphorylcholines by rat-liver microsomes”. Biochim. Biophys. Acta 144: 613-623. PMID 6078124.
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 1-acylglycerophosphocholine+O-acyltransferase
- 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