Protoporfirinogen oksidaza
Protoporfirinogen oksidaza | |||||||||
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Identifikatori | |||||||||
EC broj | 1.3.3.4 | ||||||||
CAS broj | 53986-32-6 | ||||||||
Baze podataka | |||||||||
IntEnz | IntEnz pregled | ||||||||
BRENDA | BRENDA pristup | ||||||||
ExPASy | NiceZyme pregled | ||||||||
KEGG | KEGG pristup | ||||||||
MetaCyc | metabolički put | ||||||||
PRIAM | profil | ||||||||
Strukture PBP | 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. & 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. & 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. & 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. & 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. & 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 изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
Spoljašnje veze
- Protoporphyrinogen+oxidase на US National Library of Medicine Medical Subject Headings (MeSH)