Celobioza dehidrogenaza (akceptor)
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| Celobioza dehidrogenaza (akceptor) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.1.99.18 | ||||||||
| CAS broj | 54576-85-1 | ||||||||
| 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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Celobioza dehidrogenaza (akceptor) (EC 1.1.99.18, celobiozna dehidrogenaza, celobiozna oksidoreduktaza, Phanerochaete chrysosporium celobiozna oksidoreduktaza, CBOR, celobiozna oksidaza, celobioza:kiseonik 1-oksidoreduktaza, CDH, celobioza:(akceptor) 1-oksidoreduktaza) je enzim sa sistematskim imenom celobioza:akceptor 1-oksidoreduktaza.[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju
- celobioza + akceptor celobiono-1,5-lakton + redukovani akceptor
2,6-Dihloroindofenol može da deluje kao akceptor. Ovaj enzim takođe deluje, mada sporo, na oligosaharide, laktozu i D-glukozil-1,4-beta-D-manozu. On takođe deluje kao EC 1.1.5.1, celobiozna dehidrogenaza. Enzim bele gljive Phanerochaete chrysosporium je neobičan po tome što ima dva redoks domena, pri čemu jedan sadrži flavin i drugi protohemsku grupu.
Reference[uredi | uredi kod]
- ↑ Coudray, M.-R., Canebascini, G. and Meier, H. (1982). „Characterization of a cellobiose dehydrogenase in the cellulolytic fungus porotrichum (Chrysosporium) thermophile”. Biochem. J. 203: 277-284. PMID 7103940.
- ↑ Dekker, R.F.H. (1980). „Induction and characterization of a cellobiose dehydrogenase produced by a species of Monilia”. J. Gen. Microbiol. 120: 309-316.
- ↑ Dekker, R.F.H. (1988). „Cellobiose dehydrogenase produced by Monilia sp”. Methods Enzymol. 160: 454-463.
- ↑ Habu, N., Samejima, M., Dean, J.F. and Eriksson, K.E. (1993). „Release of the FAD domain from cellobiose oxidase by proteases from cellulolytic cultures of Phanerochaete chrysosporium”. FEBS Lett. 327: 161-164. PMID 8392950.
- ↑ Baminger, U., Subramaniam, S.S., Renganathan, V. and Haltrich, D. (2001). „Purification and characterization of cellobiose dehydrogenase from the plant pathogen Sclerotium (Athelia) rolfsii”. Appl. Environ. Microbiol. 67: 1766-1774. PMID 11282631.
- ↑ Hallberg, B.M., Henriksson, G., Pettersson, G. and Divne, C. (2002). „Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase”. J. Mol. Biol. 315: 421-434. PMID 11786022.
- ↑ Ayers, A.R., Ayers, S.B. and Eriksson, K.-E. (1978). „Cellobiose oxidase, purification and partial characterization of a hemoprotein from Sporotrichum pulverulentum”. Eur. J. Biochem. 90: 171-181. PMID 710416.
- ↑ Ayers, A.R. and Eriksson, K.-E. (1982). „Cellobiose oxidase from Sporotrichum pulverulentum”. Methods Enzymol. 89: 129-135. PMID 7144569.
- ↑ Mason, M.G., Nicholls, P., Divne, C., Hallberg, B.M., Henriksson, G. and Wilson, M.T. (2003). „The heme domain of cellobiose oxidoreductase: a one-electron reducing system”. Biochim. Biophys. Acta 1604: 47-54. PMID 12686420.
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.