KEGG   ENZYME: 1.1.99.18
Entry
EC 1.1.99.18                Enzyme                                 
Name
cellobiose dehydrogenase (acceptor);
cellobiose dehydrogenase;
cellobiose oxidoreductase;
Phanerochaete chrysosporium cellobiose oxidoreductase;
CBOR;
cellobiose oxidase;
cellobiose:oxygen 1-oxidoreductase;
CDH;
cellobiose:(acceptor) 1-oxidoreductase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With unknown physiological acceptors
Sysname
cellobiose:acceptor 1-oxidoreductase
Reaction(IUBMB)
cellobiose + acceptor = cellobiono-1,5-lactone + reduced acceptor [RN:R01443 R06246]
Reaction(KEGG)
R01443 R06246(G) > R01442 R06244(G);
(other) R02365 R06247(G)
Substrate
cellobiose [CPD:C00185];
acceptor [CPD:C00028]
Product
cellobiono-1,5-lactone [CPD:C01093];
reduced acceptor [CPD:C00030]
Comment
Also acts, more slowly, on cello-oligosaccharides, lactose and D-glucosyl-1,4-beta-D-mannose. The enzyme from the white rot fungus Phanerochaete chrysosporium is unusual in having two redoxin domains, one containing a flavin and the other a protoheme group. It transfers reducing equivalents from cellobiose to two types of redox acceptor: two-electron oxidants, including redox dyes, benzoquinones, and molecular oxygen, and one-electron oxidants, including semiquinone species, iron(II) complexes, and the model acceptor cytochrome c [9]. 2,6-Dichloroindophenol can act as acceptor in vitro.
History
EC 1.1.99.18 created 1983, modified 2002 (EC 1.1.5.1 created 1983, incorporated 2002, EC 1.1.3.25 created 1986, incorporated 2005)
Orthology
K19069  cellobiose dehydrogenase (acceptor)
Genes
NCRNCU00206(cdh-1) NCU05923(cdh-2)
NTENEUTE1DRAFT129729(NEUTE1DRAFT_129729) NEUTE1DRAFT50117(NEUTE1DRAFT_50117)
SMPSMAC_02223 SMAC_06953 SMAC_08924
PANPODANSg3842 PODANSg4789 PODANSg891
TTTTHITE_123924 THITE_158792 THITE_59724
MTMMYCTH_111388(cbdA) MYCTH_58125 MYCTH_81925
CTHRCTHT_0020370 CTHT_0022390
MGRMGG_07569 MGG_08487 MGG_09189 MGG_11036 MGG_13809
PPEIPpBr36_02475 PpBr36_03722 PpBr36_05357 PpBr36_07515 PpBr36_10735
TMNUCRPA7_2781 UCRPA7_378
SSCKSPSK_01587 SPSK_04896
FGRFGSG_02917 FGSG_03742 FGSG_04872 FGSG_05983 FGSG_09085
FPUFPSE_02995 FPSE_04011 FPSE_06706 FPSE_07371 FPSE_08439
FVRFVEG_03526 FVEG_04610 FVEG_08702 FVEG_13307 FVEG_13310
FOXFOXG_05670 FOXG_07688 FOXG_09780 FOXG_15834 FOXG_15839
NHENECHADRAFT_37056 NECHADRAFT_78826 NECHADRAFT_97389
MAWMAC_02953
MAJMAA_07725
CMTCCM_06091
PLJVFPFJ_10450
VALVDBG_02986 VDBG_06351 VDBG_09842 VDBG_10097
VDAVDAG_03501 VDAG_03896 VDAG_05396
CFJCFIO01_00885 CFIO01_01228 CFIO01_01926 CFIO01_04006 CFIO01_08348
CHIGCH63R_08769 CH63R_09712
SAPOSAPIO_CDS8557 SAPIO_CDS9070
ELAUCREL1_10476 UCREL1_1467 UCREL1_1483 UCREL1_7373 UCREL1_764 UCREL1_9722
PFYPFICI_02482 PFICI_05027 PFICI_06779 PFICI_08637 PFICI_09039 PFICI_11856
SSLSS1G_05151 SS1G_06264 SS1G_07863 SS1G_13051
BFUBCIN_01g00640 BCIN_05g06510 BCIN_12g02910 BCIN_15g01170
MBEMBM_01462 MBM_01896 MBM_04275 MBM_06962 MBM_09959
PSCOLY89DRAFT_266653 LY89DRAFT_739447 LY89DRAFT_742888 LY89DRAFT_780009
GLZGLAREA_00977 GLAREA_03815 GLAREA_05733
ANIAN7230.2
AFMAFUA_2G01180 AFUA_2G17620
ACTACLA_076510 ACLA_094490
NFINFIA_033480 NFIA_093020
AORAO090102000058 AO090113000054
ANGANI_1_168174(An10g00390) ANI_1_2878024(An02g09270)
AFVAFLA_009770 AFLA_011511
ALUCAKAW2_10793A AKAW2_71039S
ACHEACHE_20113S ACHE_40057A
APUUAPUU_20182S APUU_71209S
PCSPc20g04990
PDPPDIP_07720
TRGTRUGW13939_09239
PNOSNOG_02444 SNOG_10188 SNOG_11248 SNOG_13073
PTEPTT_04706 PTT_09415 PTT_12135
BZECOCCADRAFT_111999 COCCADRAFT_3787 COCCADRAFT_81268
BSCCOCSADRAFT_196954 COCSADRAFT_199941 COCSADRAFT_34768
BORCOCMIDRAFT_2145 COCMIDRAFT_25331 COCMIDRAFT_35852 COCMIDRAFT_91230
AALTCC77DRAFT_1010416 CC77DRAFT_950453 CC77DRAFT_959348
ZTRMYCGRDRAFT_62587(CDH)
PFJMYCFIDRAFT_215593 MYCFIDRAFT_77759
FFUCLAFUR5_06958 CLAFUR5_14150
NPAUCRNP2_206 UCRNP2_2863 UCRNP2_3739 UCRNP2_5184 UCRNP2_7189
TMLGSTUM_00008390001
TVSTRAVEDRAFT_73596
DSQDICSQDRAFT_153749
PCOPHACADRAFT_259608
SHSSTEHIDRAFT_62168
HIRHETIRDRAFT_157537(cdh1)
PSQPUNSTDRAFT_107198
ADLAURDEDRAFT_161830
FMEFOMMEDRAFT_139496
GTRGLOTRDRAFT_113732
MPRMPER_11289
MRRMoror_16128 Moror_1980
MOREE1B28_007783(CDH1)
CCICC1G_09923
SCMSCHCODRAFT_114791
ABPAGABI1DRAFT107890(AGABI1DRAFT_107890)
ABVAGABI2DRAFT188178(AGABI2DRAFT_188178)
CPUTCONPUDRAFT_131886 CONPUDRAFT_140809
SLASERLADRAFT_453176(CDH2) SERLADRAFT_491377
PIFPITG_00805 PITG_07303 PITG_16169 PITG_18951
PSOJPHYSODRAFT_316871 PHYSODRAFT_346580 PHYSODRAFT_482381 PHYSODRAFT_517891 PHYSODRAFT_557002
SPARSPRG_01483 SPRG_01485 SPRG_01486 SPRG_13203
RHWBFN03_04975
 » show all
Reference
1  [PMID:7103940]
  Authors
Coudray MR, Canevascini G, Meier H.
  Title
Characterization of a cellobiose dehydrogenase in the cellulolytic fungus Sporotrichum (Chrysosporium) thermophile.
  Journal
Biochem J 203:277-84 (1982)
DOI:10.1042/bj2030277
Reference
2
  Authors
Dekker, R.F.H.
  Title
Induction and characterization of a cellobiose dehydrogenase produced by a species of Monilia.
  Journal
J Gen Microbiol 120:309-316 (1980)
Reference
3
  Authors
Dekker, R.F.H.
  Title
Cellobiose dehydrogenase produced by Monilia sp.
  Journal
Methods Enzymol 160:454-463 (1988)
Reference
4  [PMID:8392950]
  Authors
Habu N, Samejima M, Dean JF, Eriksson KE.
  Title
Release of the FAD domain from cellobiose oxidase by proteases from cellulolytic cultures of Phanerochaete chrysosporium.
  Journal
FEBS Lett 327:161-4 (1993)
DOI:10.1016/0014-5793(93)80162-N
Reference
5  [PMID:11282631]
  Authors
Baminger U, Subramaniam SS, Renganathan V, Haltrich D.
  Title
Purification and characterization of cellobiose dehydrogenase from the plant pathogen Sclerotium (Athelia) rolfsii.
  Journal
Appl Environ Microbiol 67:1766-74 (2001)
DOI:10.1128/AEM.67.4.1766-1774.2001
Reference
6  [PMID:11786022]
  Authors
Hallberg BM, Henriksson G, Pettersson G, Divne C.
  Title
Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase.
  Journal
J Mol Biol 315:421-34 (2002)
DOI:10.1006/jmbi.2001.5246
Reference
7  [PMID:710416]
  Authors
Ayers AR, Ayers SB, Eriksson KE.
  Title
Cellobiose oxidase, purification and partial characterization of a hemoprotein from Sporotrichum pulverulentum.
  Journal
Eur J Biochem 90:171-81 (1978)
DOI:10.1111/j.1432-1033.1978.tb12588.x
Reference
8  [PMID:7144569]
  Authors
Ayers AR, Eriksson KE.
  Title
Cellobiose oxidase from Sporotrichum pulverulentum.
  Journal
Methods Enzymol 89 Pt D:129-35 (1982)
DOI:10.1016/s0076-6879(82)89022-8
Reference
9  [PMID:12686420]
  Authors
Mason MG, Nicholls P, Divne C, Hallberg BM, Henriksson G, Wilson MT.
  Title
The heme domain of cellobiose oxidoreductase: a one-electron reducing system.
  Journal
Biochim Biophys Acta 1604:47-54 (2003)
DOI:10.1016/S0005-2728(03)00023-9
Other DBs
ExplorEnz - The Enzyme Database: 1.1.99.18
IUBMB Enzyme Nomenclature: 1.1.99.18
ExPASy - ENZYME nomenclature database: 1.1.99.18
BRENDA, the Enzyme Database: 1.1.99.18
CAS: 54576-85-1
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