Polivinil alkohol dehidrogenaza (citohrom)
(Preusmjereno sa stranice PVADH)
Polivinil alkohol dehidrogenaza (citohrom) (EC 1.1.2.6, PVA dehidrogenaza, PVADH) je enzim sa sistematskim imenom polivinil alkohol:fericitohrom-c oksidoreduktaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Polivinil alkohol dehidrogenaza (citohrom) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.1.2.6 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- polivinil alkohol + fericitohrom c oksidovani polivinil alkohol + ferocitohrom c + H+
Ovaj enzim učestvuje u degradaciji bakterijskih polivinilnih alkohola. Neke gram-negativne bakterije razgrađuju polivinilni alkohol putem njegovog unosa u periplazmatični prostor, gde se on oksiduje dejstvom polivinil alkoholne dehidrogenaza, enzima koji je spregnut sa respiratornim lancem putem citohroma c. Ovaj enzim sadrži pirolohinolin hinonski kofaktor.
Reference uredi
- ↑ Shimao, M., Ninomiya, K., Kuno, O., Kato, N. and Sakazawa, C. (1986). „Existence of a novel enzyme, pyrroloquinoline quinone-dependent polyvinyl alcohol dehydrogenase, in a bacterial symbiont, Pseudomonas sp. strain VM15C”. Appl. Environ. Microbiol. 51: 268-268. PMID 3513704.
- ↑ Shimao, M., Onishi, S., Kato, N. and Sakazawa, C. (1989). „Pyrroloquinoline quinone-dependent cytochrome reduction in polyvinyl alcohol-degrading Pseudomonas sp strain VM15C”. Appl. Environ. Microbiol. 55: 275-278. PMID 16347841.
- ↑ Mamoto, R., Hu, X., Chiue, H., Fujioka, Y. and Kawai, F. (2008). „Cloning and expression of soluble cytochrome c and its role in polyvinyl alcohol degradation by polyvinyl alcohol-utilizing Sphingopyxis sp. strain 113P3”. J. Biosci. Bioeng. 105: 147-151. PMID 18343342.
- ↑ Hirota-Mamoto, R., Nagai, R., Tachibana, S., Yasuda, M., Tani, A., Kimbara, K. and Kawai, F. (2006). „Cloning and expression of the gene for periplasmic poly(vinyl alcohol) dehydrogenase from Sphingomonas sp. strain 113P3, a novel-type quinohaemoprotein alcohol dehydrogenase”. Microbiology 152: 1941-1949. PMID 16804170.
- ↑ Hu, X., Mamoto, R., Fujioka, Y., Tani, A., Kimbara, K. and Kawai, F. (2008). „The pva operon is located on the megaplasmid of Sphingopyxis sp. strain 113P3 and is constitutively expressed, although expression is enhanced by PVA”. Appl. Microbiol. Biotechnol. 78: 685-693. PMID 18214469.
- ↑ Kawai, F. and Hu, X. (2009). „Biochemistry of microbial polyvinyl alcohol degradation”. Appl. Microbiol. Biotechnol. 84: 227-237. PMID 19590867.
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.