Polienoinska masno kiselinska izomeraza
| Polienoinska masno kiselinska izomeraza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 5.3.3.13 | ||||||||
| CAS broj | 159002-84-3 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Polienoinska masno kiselinska izomeraza (EC 5.3.3.13, PFI, eikosapentaenoat cis-Delta5,8,11,14,17-eikosapentaenoat cis-Delta5-trans-Delta7,9-cis-Delta14,17 izomeraza, (5Z,8Z,11Z,14Z,17Z)-eikosapentaenoat Delta8,11-Delta7,8-izomeraza, (5Z,8Z,11Z,14Z,17Z)-eikosapentaenoat Delta8,11-Delta7,9-izomeraza (formira trans dvostruku vezu)) je enzim sa sistematskim imenom (5Z,8Z,11Z,14Z,17Z)-ikosapentaenoat Delta8,11-Delta7,9-izomeraza (formira trans dvostruku vezu).[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (5Z,8Z,11Z,14Z,17Z)-ikosapentaenoat (5Z,7E,9E,14Z,17Z)-ikosapentaenoat
Enzim iz crvene alge Ptilota filicina katalizuje izomerizaciju diena.
Reference
- ↑ Wise, M.L., Hamberg, M. and Gerwick, W.H. (1994). „Biosynthesis of conjugated fatty acids by a novel isomerase from the red marine alga Ptilota filicina”. Biochemistry 33: 15223-15232. PMID 7803384.
- ↑ Wise, M.L., Soderstrom, K., Murray, T.F. and Gerwick, W.H. (1996). „Synthesis and cannabinoid receptor binding activity of conjugated triene anandamide, a novel eicosanoid”. Experientia 52: 88-92. PMID 8575565.
- ↑ Wise, M.L., Rossi, J. and Gerwick, W.H. (1997). „Binding site characterization of polyenoic fatty-acid isomerase from the marine alga Ptilota filicina”. Biochemistry 36: 2985-2992. PMID 9062129.
- ↑ Zheng, W., Wise, M.L., Wyrick, A., Metz, J.G., Yuan, L. and Gerwick, W.H. (2002). „Polyenoic fatty-acid isomerase from the marine red alga Ptilota filicina: protein characterization and functional expression of the cloned cDNA”. Arch. Biochem. Biophys. 401: 11-20. PMID 12054482.
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 Polyenoic+fatty+acid+isomerase
- 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
