Alkohol dehidrogenaza (azurin)
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Alkohol dehidrogenaza (azurin) | |||||||||
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Identifikatori | |||||||||
EC broj | 1.1.9.1 | ||||||||
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 (azurin) (EC 1.1.9.1, tip II hinoproteinska alkoholna dehidrogenaza, hinohemoproteinska etanolna dehidrogenaza, QHEDH, ADHIIB) je enzim sa sistematskim imenom alkohol:azurin oksidoreduktaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- primarni alkohol + azurin aldehid + redukovani azurin
Ovaj rastvorni, periplazmični hinohemoprotein sadrži PQQ i hem c. On se javlja u Comamonas i Pseudomonas. Za njegovo dejstvo nije neophodan aminski aktivator. On oksiduje širok opsed primarnih i sekundarnih alkohola, kao i aldehide i velike supstrate poput sterola. Metanol nije njegov supstrat.
Reference[uredi | uredi kod]
- ↑ Groen, B.W., van Kleef, M.A. and Duine, J.A. (1986). „Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni”. Biochem. J. 234: 611-615. PMID 3521592.
- ↑ de Jong, G.A., Caldeira, J., Sun, J., Jongejan, J.A., de Vries, S., Loehr, T.M., Moura, I., Moura, J.J. and Duine, J.A. (1995). „Characterization of the interaction between PQQ and heme c in the quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni”. Biochemistry 34: 9451-9458. PMID 7626615.
- ↑ 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.
- ↑ Matsushita, K., Yamashita, T., Aoki, N., Toyama, H. and Adachi, O. (1999). „Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory chain of Pseudomonas putida HK5”. Biochemistry 38: 6111-6118. PMID 10320337.
- ↑ Chen, Z.W., Matsushita, K., Yamashita, T., Fujii, T.A., Toyama, H., Adachi, O., Bellamy, H.D. and Mathews, F.S. (2002). „Structure at 1.9 Å resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5”. Structure 10: 837-849. PMID 12057198.
- ↑ Oubrie, A., Rozeboom, H.J., Kalk, K.H., Huizinga, E.G. and Dijkstra, B.W. (2002). „Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer”. J. Biol. Chem. 277: 3727-3732. PMID 11714714.
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.