Alkohol dehidrogenaza (citohrom c)
Alkohol dehidrogenaza (citohrom c) | |||||||||
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Identifikatori | |||||||||
EC broj | 1.1.2.8 | ||||||||
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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Alkohol dehidrogenaza (citohrom c) (EC 1.1.2.8, tip I hinoprotein alkohol dehidrogenaza, hinoprotein etanol dehidrogenaza) je enzim sa sistematskim imenom alkohol:citohrom c oksidoreduktaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- primarni alkohol + 2 fericitohrom c aldehid + 2 ferocitohrom c + 2 H+
Ovaj enzim je periplazmični hinoprotein koji sadrži PQQ. On je prisutan kod Pseudomonas i Rhodopseudomonas. Enzim iz Pseudomonas aeruginosa koristi specifični induktivni citohrom c550 kao elektronski akceptor. On deluje na širok opseg primarnih i sekundarnih alkohola, ali ne na metanol. On ima homodimernu strukturu, što je u kontrastu sa heterotetramernom strukturom EC 1.1.2.7, metanol dehidrogenaze (citohroma ac). On se rutinski testira sa fenazin metosulfatom kao elektronskim akceptorom. Njegovu aktivnost stimulišu amonijak i amini. Poput svih drugih dehidrogenaza hinoproteinskih alkohola, on ima strukturu propelera sa osam lopatica, jon kalcijuma vezan za PQQ u aktivnom mestu i jednu neobičnu strukturu disulfidnog prstena u blizini PQQ-a.
Reference[uredi | uredi kod]
- ↑ Rupp, M. and Gorisch, H. (1988). „Purification, crystallisation and characterization of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa”. Biol. Chem. Hoppe-Seyler 369: 431-439. PMID 3144289.
- ↑ Toyama, H., Fujii, A., Matsushita, K., Shinagawa, E., Ameyama, M. and Adachi, O. (1995). „Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols”. J. Bacteriol. 177: 2442-2450. PMID 7730276.
- ↑ Schobert, M. and Gorisch, H. (1999). „Cytochrome c550 is an essential component of the quinoprotein ethanol oxidation system in Pseudomonas aeruginosa: cloning and sequencing of the genes encoding cytochrome c550 and an adjacent acetaldehyde dehydrogenase”. Microbiology 145: 471-481. PMID 10075429.
- ↑ Keitel, T., Diehl, A., Knaute, T., Stezowski, J.J., Hohne, W. and Gorisch, H. (2000). „X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity”. J. Mol. Biol. 297: 961-974. PMID 10736230.
- ↑ Kay, C.W., Mennenga, B., Gorisch, H. and Bittl, R. (2004). „Characterisation of the PQQ cofactor radical in quinoprotein ethanol dehydrogenase of Pseudomonas aeruginosa by electron paramagnetic resonance spectroscopy”. FEBS Lett. 564: 69-72. PMID 15094044.
- ↑ Mennenga, B., Kay, C.W. and Gorisch, H. (2009). „Quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: the unusual disulfide ring formed by adjacent cysteine residues is essential for efficient electron transfer to cytochrome c550”. Arch. Microbiol. 191: 361-367. PMID 19224199.
Literatura[uredi | uredi kod]
- 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.