Hem oksigenaza (deciklizacija)
| Hem oksigenaza (deciklizacija) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Dimer hem oksigenaze I (čovjek) | |||||||||
| Identifikatori | |||||||||
| EC broj | 1.14.99.3 | ||||||||
| CAS broj | 9059-22-7 | ||||||||
| 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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Hem oksigenaza (deciklizacija) (EC 1.14.99.3, ORP33 proteini, hem oksigenaza, hem oksidaza, hem oksidaza) je enzim sa sistematskim imenom hem,vodonik-donor:kiseonik oksidoreduktaza (alfa-meten-oksidacija, hidroksilacija).[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- hem + 3 AH2 + 3 O2 biliverdin + Fe2+ + CO + 3 A + 3H2O
Za rad ovog enzima je neophodan NAD(P)H i EC 1.6.2.4, NADPH-hemoproteinska reduktaza. Terminalni atomi kiseonika koji nisu inkorporirani u karbonilne grupe pirolnih prstena A i B biliverdina su izvedeni dva zasebna molekula kiseonika.
Reference
- ↑ Maines, M.D., Ibrahim, N.G. and Kappas, K. (1977). „Solubilization and partial purification of heme oxygenase from rat liver”. J. Biol. Chem. 252: 5900-5903. PMID 18477.
- ↑ Sunderman, F.W., Jr., Downs, J.R., Reid, M.C. and Bibeau, L.M. (1982). „Gas-chromatographic assay for heme oxygenase activity”. Clin. Chem. 28: 2026-2032. PMID 6897023.
- ↑ Yoshida, T., Takahashi, S. and Kikuchi, J. (1974). „Partial purification and reconstitution of the heme oxygenase system from pig spleen microsomes”. J. Biochem. (Tokyo) 75: 1187-1191. PMID 4370250.
- ↑ Noguchi, M., Yoshida, T. and Kikuchi, G. (1979). „Specific requirement of NADPH-cytochrome c reductase for the microsomal heme oxygenase reaction yielding biliverdin IX α”. FEBS Lett. 98: 281-284. PMID 105935.
- ↑ Lad, L., Schuller, D.J., Shimizu, H., Friedman, J., Li, H., Ortiz de Montellano, P.R. and Poulos, T.L. (2003). „Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1”. J. Biol. Chem. 278: 7834-7843. PMID 12500973.
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 Heme+oxygenase
- 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
