Celobioza dehidrogenaza (akceptor)

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
Pretraga PMC articles PubMed articles NCBI Protein search

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 ${\displaystyle \rightleftharpoons }$ 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

1. 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. 
2. Dekker, R.F.H. (1980). „Induction and characterization of a cellobiose dehydrogenase produced by a species of Monilia”. J. Gen. Microbiol. 120: 309-316. 
3. Dekker, R.F.H. (1988). „Cellobiose dehydrogenase produced by Monilia sp”. Methods Enzymol. 160: 454-463. 
4. 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. 
5. 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. 
6. 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. 
7. 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. 
8. Ayers, A.R. and Eriksson, K.-E. (1982). „Cellobiose oxidase from Sporotrichum pulverulentum”. Methods Enzymol. 89: 129-135. PMID 7144569. 
9. 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

• 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. 

Vanjske veze

• MeSH Cellobiose+dehydrogenase+(acceptor)