Lipoksigenaza
| Lipoksigenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifikatori | |||||||||
| EC broj | 1.13.11.12 | ||||||||
| CAS broj | 9029-60-1 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Lipoksigenaza (EC 1.13.11.12, 13-lipoksidaza, karotenksa oksidaza, 13-lipoperoksidaza, masna oksidaza, 13-lipoksidaza, lionoleat:O2 13-oksidoreduktaza) je enzim sa sistematskim imenom linoleat:kiseonik 13-oksidoreduktaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (1) linoleat + O2 (9Z,11E,13S)-13-hidroperoksioktadeka-9,11-dienoat
- (2) alfa-linolenat + O2 (9Z,11E,13S,15Z)-13-hidroperoksioktadeka-9,11,15-trienoat
Ovaj enzim sadrži nehemno gvožđe. Rasprostanjena biljna lipoksigenaza oksiduje linoleat i alfa-linolenat, dve najzastupljenije polinezasićene masne kiseline kod biljki, putem umetanja molekularnog kiseonika na C-13 poziciju (S)-konfiguracijom.
Reference
- ↑ Christopher, J., Pistorius, E. and Axelrod, B. (1970). „Isolation of an enzyme of soybean lipoxidase”. Biochim. Biophys. Acta 198: 12-19. PMID 5461103.
- ↑ Theorell, H., Holman, R.T. and Åkesson, Å. (1947). „Crystalline lipoxidase”. Acta Chem. Scand. 1: 571-576. PMID 18907700.
- ↑ Zimmerman, D.C. (1970). „Specificity of flaxseed lipoxidase”. Lipids 5: 392-397. PMID 5447012.
- ↑ Royo, J., Vancanneyt, G., Perez, A.G., Sanz, C., Stormann, K., Rosahl, S. and Sanchez-Serrano, J.J. (1996). „Characterization of three potato lipoxygenases with distinct enzymatic activities and different organ-specific and wound-regulated expression patterns”. J. Biol. Chem. 271: 21012-21019. PMID 8702864.
- ↑ Bachmann, A., Hause, B., Maucher, H., Garbe, E., Voros, K., Weichert, H., Wasternack, C. and Feussner, I. (2002). „Jasmonate-induced lipid peroxidation in barley leaves initiated by distinct 13-LOX forms of chloroplasts”. Biol. Chem. 383: 1645-1657. PMID 12452441.
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 Linoleate+13S-lipoxygenase
- 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
