Cellobiose dehydrogenase (acceptor)

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cellobiose dehydrogenase (acceptor)
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

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 located in separate domains. It makes the enzyme to one of the more complex extracellular oxidoreductases. It is produced by wood degrading organisms.[1]

Structural studies[edit]

To date, structures of the separated flavin and heme containing domains were reported (PDB accession codes 1NAA[2] and 1PL3[3]). In 2015, full-length structures of the enzyme were resolved (accession codes 4QI6 and 4QI7).[4]

References[edit]

  1. ^ Westermark, Ulla; Eriksson, Karl-Erik; Daasvatn, Kari; Liaaen-Jensen, Synnøve; Enzell, Curt R.; Mannervik, Bengt. "Cellobiose:Quinone Oxidoreductase, a New Wood-degrading Enzyme from White-rot Fungi.". Acta Chemica Scandinavica. 28b: 209–214. doi:10.3891/acta.chem.scand.28b-0209. 
  2. ^ Martin Hallberg, B; Henriksson, Gunnar; Pettersson, Göran; Divne, Christina (2002-01-18). "Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase1". Journal of Molecular Biology. 315 (3): 421–434. doi:10.1006/jmbi.2001.5246. PMID 11786022. 
  3. ^ Rotsaert, Frederik A. J.; Hallberg, B. Martin; Vries, Simon de; Moenne-Loccoz, Pierre; Divne, Christina; Renganathan, V.; Gold, Michael H. (2003-08-29). "Biophysical and Structural Analysis of a Novel Heme b Iron Ligation in the Flavocytochrome Cellobiose Dehydrogenase". Journal of Biological Chemistry. 278 (35): 33224–33231. doi:10.1074/jbc.M302653200. ISSN 0021-9258. PMID 12796496. 
  4. ^ Tan TC, Kracher D, Gandini R, Sygmund C, Kittl R, Haltrich D, Hällberg BM, Ludwig R, Divne C (July 2015). "Structural basis for cellobiose dehydrogenase action during oxidative cellulose degradation". Nat. Commun. 6: 7542. doi:10.1038/ncomms8542. PMC 4507011Freely accessible. PMID 26151670.