Protoporfirinogen oksidaza
| Protoporfirinogen oksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifikatori | |||||||||
| EC broj | 1.3.3.4 | ||||||||
| CAS broj | 53986-32-6 | ||||||||
| 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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Protoporfirinogen oksidaza (EC 1.3.3.4, protoporfirinogenska IX oksidaza, protoporfirinogenaza, PPO, Protox, HemG, HemY) je enzim sa sistematskim imenom protoporfirinogen-IX:kiseonik oksidoreduktaza.[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju
- protoporfirinogen IX + 3 O2 protoporfirin IX + 3H2O2
Ovaj enzim je najmanje zastupljen u biosintezi hlorofila i hema. Postoje dva izoenzima kod biljki: jedan u plastidima i drugi u mitohondrijama. On je meta ftalimidnog i difenileterskog tipa herbicida.
Reference
- ↑ Poulson, R. (1976). „The enzymic conversion of protoporphyrinogen IX to protoporphyrin IX in mammalian mitochondria”. J. Biol. Chem. 251: 3730-3733. PMID 6461.
- ↑ Poulson, R. and Polglase, W.J. (1975). „The enzymic conversion of protoporphyrinogen IX to protoporphyrin IX. Protoporphyrinogen oxidase activity in mitochondrial extracts of Saccharomyces cerevisiae”. J. Biol. Chem. 250: 1269-1274. PMID 234450.
- ↑ Dailey, H.A. and Dailey, T.A. (1996). „Protoporphyrinogen oxidase of Myxococcus xanthus. Expression, purification, and characterization of the cloned enzyme”. J. Biol. Chem. 271: 8714-8718. PMID 8621504.
- ↑ Wang, K.F., Dailey, T.A. and Dailey, H.A. (2001). „Expression and characterization of the terminal heme synthetic enzymes from the hyperthermophile Aquifex aeolicus”. FEMS Microbiol. Lett. 202: 115-119. PMID 11506917.
- ↑ Corrigall, A.V., Siziba, K.B., Maneli, M.H., Shephard, E.G., Ziman, M., Dailey, T.A., Dailey, H.A. (1998). „, Kirsch. R.E. and Meissner, P.N. Purification of and kinetic studies on a cloned protoporphyrinogen oxidase from the aerobic bacterium Bacillus subtilis”. Arch. Biochem. Biophys. 358: 251-256. PMID 9784236.
- ↑ Ferreira, G.C. and Dailey, H.A. (1988). „Mouse protoporphyrinogen oxidase. Kinetic parameters and demonstration of inhibition by bilirubin”. Biochem. J. 250: 597-603. PMID 2451512.
- ↑ Dailey, T.A. and Dailey, H.A. (1996). „Human protoporphyrinogen oxidase: expression, purification, and characterization of the cloned enzyme”. Protein Sci. 5: 98-105. PMID 8771201.
- ↑ Che, F.S., Watanabe, N., Iwano, M., Inokuchi, H., Takayama, S., Yoshida, S. and Isogai, A. (2000). „Molecular characterization and subcellular localization of protoporphyrinogen oxidase in spinach chloroplasts”. Plant Physiol. 124: 59-70. PMID 10982422.
- ↑ Dailey, T.A. and Dailey, H.A. (1998). „Identification of an FAD superfamily containing protoporphyrinogen oxidases, monoamine oxidases, and phytoene desaturase. Expression and characterization of phytoene desaturase of Myxococcus xanthus”. J. Biol. Chem. 273: 13658-13662. PMID 9593705.
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 Protoporphyrinogen+oxidase
- 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
