Cellobiose dehydrogenase (acceptor)
| cellobiose dehydrogenase (acceptor) | |||||||||
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| Identifiers | |||||||||
| EC number | 1.1.99.18 | ||||||||
| CAS number | 54576-85-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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In enzymology, a cellobiose dehydrogenase (acceptor) (EC 1.1.99.18) is an enzyme that catalyzes the chemical reaction
- cellobiose + acceptor
cellobiono-1,5-lactone + reduced acceptor
Thus, the two substrates of this enzyme are cellobiose and acceptor, whereas its two products are cellobiono-1,5-lactone and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is cellobiose:acceptor 1-oxidoreductase. Other names in common use include cellobiose dehydrogenase, cellobiose oxidoreductase, Phanerochaete chrysosporium cellobiose oxidoreductase, CBOR, cellobiose oxidase, cellobiose:oxygen 1-oxidoreductase, CDH, and cellobiose:(acceptor) 1-oxidoreductase. It employs sometimes one cofactor, FAD, but in most cases both a heme and a FAD. It makes the enzyme to one of the more complex extracellulae oxidoreductases. It is produced by wood degrading organisms.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1NAA and 1PL3.
References
- Coudray MR, Canevascini G, Meier H (1982). "Characterization of a cellobiose dehydrogenase in the cellulolytic fungus Sporotrichum (Chrysosporium) thermophile". Biochem. J. 203 (1): 277–84. PMC 1158220. PMID 7103940.
- Dekker RFH (1980). "Induction and characterization of a cellobiose dehydrogenase produced by a species of Monilia". J. Gen. Microbiol. 120: 309–316. doi:10.1099/00221287-120-2-309.
- Dekker RFH (1988). "Cellobiose dehydrogenase produced by Monilia sp". Methods Enzymol. Methods in Enzymology 160: 454–463. doi:10.1016/0076-6879(88)60154-6. ISBN 978-0-12-182061-9.
- Habu N, Samejima M, Dean JF, Eriksson KE (1993). "Release of the FAD domain from cellobiose oxidase by proteases from cellulolytic cultures of Phanerochaete chrysosporium". FEBS Lett. 327 (2): 161–4. doi:10.1016/0014-5793(93)80162-N. PMID 8392950.
- Baminger U, Subramaniam SS, Renganathan V, Haltrich D (2001). "Purification and Characterization of Cellobiose Dehydrogenase from the Plant Pathogen Sclerotium (Athelia) rolfsii". Appl. Environ. Microbiol. 67 (4): 1766–74. doi:10.1128/AEM.67.4.1766-1774.2001. PMC 92795. PMID 11282631.
- Hallberg BM, Henriksson G, Pettersson G, Divne C (2002). "Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase". J. Mol. Biol. 315 (3): 421–34. doi:10.1006/jmbi.2001.5246. PMID 11786022.
- Ayers AR, Ayers SB, Eriksson KE (1978). "Cellobiose oxidase, purification and partial characterization of a hemoprotein from Sporotrichum pulverulentum". Eur. J. Biochem. 90 (1): 171–81. doi:10.1111/j.1432-1033.1978.tb12588.x. PMID 710416.
- Ayers AR, Eriksson KE (1982). "Cellobiose oxidase from Sporotrichum pulverulentum". Methods. Enzymol. 89 Pt D: 129–35. doi:10.1016/s0076-6879(82)89022-8. PMID 7144569.
- Mason MG, Nicholls P, Divne C, Hallberg BM, Henriksson G, Wilson MT (2003). "The heme domain of cellobiose oxidoreductase: a one-electron reducing system". Biochim. Biophys. Acta 1604 (1): 47–54. doi:10.1016/s0005-2728(03)00023-9. PMID 12686420.
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