Gliceronfosfat O-aciltransferaza
| Gliceron-fosfat O-aciltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.3.1.42 | ||||||||
| CAS broj | 37257-19-5 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
| Gliceronfosfat O-aciltransferaza | |
|---|---|
| Identifikatori | |
| Simbol | GNPAT |
| Entrez | 8443 |
| Hugo | 4416 |
| OMIM | 602744 |
| RefSek | NM_014236 |
| UniProt | O15228 |
| Drugi podaci | |
| EC broj | 2.3.1.42 |
| Lokus | Hrom. 1 q42 |
Gliceron-fosfat O-aciltransferaza (EC 2.3.1.42, dihidroksiaceton fosfatna aciltransferaza) je enzim sa sistematskim imenom acil-KoA:gliceron-fosfat O-aciltransferaza.[1][2][3] Ovaj enzim katalizuje sledeću hemijsku reakciju
- acil-KoA + gliceron fosfat KoA + acilgliceron fosfat
Ovaj enzim je membranski protein. On koristi KoA derivate palmitata, stearata i oleata. Najaktivniji je na palmitoil-KoA.
Gliceronfosfat O-aciltransferaza je enzim vezan za bolest rizomelna hondrodisplazija punktata, tip 2.[4]
Reference
- ↑ Ballas, L.M. and Bell, R.M. (1981). „Topography of glycerolipid synthetic enzymes. Synthesis of phosphatidylserine, phosphatidylinositol and glycerolipid intermediates occurs on the cytoplasmic surface of rat liver microsomal vesicles”. Biochim. Biophys. Acta 665: 586-595. PMID 6271231.
- ↑ Declercq, P.E., Haagsman, H.P., Van Veldhoven, P., Debeer, L.J., Van Golde, L.M.G. and Mannaerts, G.P. (1984). „Rat liver dihydroxyacetone-phosphate acyltransferases and their contribution to glycerolipid synthesis”. J. Biol. Chem. 259: 9064-9075. PMID 6746639.
- ↑ Hajra, A.K. (1968). „Biosynthesis of acyl dihydroxyacetone phosphate in guinea pig liver mitochondria”. J. Biol. Chem. 243: 3458-3465. PMID 5656381.
- ↑ Jan Velišek and Karel Cejpek. „Biosynthesis of Food Constituents: Lipids. 2. Triacylglycerols, Glycerophospholipids, and Glyceroglycolipids”. Czech J. Food Sci. 24: 241–254.
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
- 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
