Alkohol dehidrogenaza (azurin)
(Preusmjereno sa stranice Tp II hinoproteinska alkoholna dehidrogenaza)
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
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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- 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
- ↑ 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
- 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.