KEGG ENZYME: 1.1.99.18

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

NCR:	NCU00206(cdh-1) NCU05923(cdh-2)

NTE:	NEUTE1DRAFT129729(NEUTE1DRAFT_129729) NEUTE1DRAFT50117(NEUTE1DRAFT_50117)

SMP:	SMAC_02223 SMAC_06953 SMAC_08924

PAN:	PODANSg3842 PODANSg4789 PODANSg891

PBEL:

QC761_000280 QC761_611360 QC761_702650

PPSD:

QC762_000280 QC762_611360 QC762_702650

PPSP:

QC763_000280 QC763_611360 QC763_702650

PPSA:

QC764_000280 QC764_611360 QC764_702650

TTT:	THITE_123924 THITE_158792 THITE_59724

MTM:	MYCTH_111388(cbdA) MYCTH_58125 MYCTH_81925

CTHR:

CTHT_0020370 CTHT_0022390

MGR:	MGG_07569 MGG_08487 MGG_09189 MGG_11036 MGG_13809

PPEI:

PpBr36_02475 PpBr36_03722 PpBr36_05357 PpBr36_07515 PpBr36_10735

PGRI:

PgNI_00122 PgNI_02001 PgNI_03000 PgNI_09374

TMN:	UCRPA7_2781 UCRPA7_378

SSCK:

SPSK_01587 SPSK_04896

FGR:	FGSG_02917 FGSG_03742 FGSG_04872 FGSG_05983 FGSG_09085

FPU:	FPSE_02995 FPSE_04011 FPSE_06706 FPSE_07371 FPSE_08439

FPOA:

FPOAC1_005267 FPOAC1_006145 FPOAC1_009957

FVN:	FVRRES_05809 FVRRES_06747 FVRRES_10614

FVR:	FVEG_03526 FVEG_04610 FVEG_08702 FVEG_13307 FVEG_13310

FOX:	FOXG_05670 FOXG_07688 FOXG_09780 FOXG_15834 FOXG_15839

NHE:	NECHADRAFT_37056 NECHADRAFT_78826 NECHADRAFT_97389

FFC:	NCS54_00464300 NCS54_00533900 NCS54_01355200

FKR:	NCS57_00469200 NCS57_01344500

FMU:	J7337_009135 J7337_009138 J7337_012636

MAW:

MAC_02953

MAJ:

MAA_07725

PCHM:

VFPPC_05303

CMT:

CCM_06091

AMUS:

LMH87_005271

PLJ:	VFPFJ_10450

PTKZ:

JDV02_008163

VAL:	VDBG_02986 VDBG_06351 VDBG_09842 VDBG_10097

VDA:	VDAG_03501 VDAG_03896 VDAG_05396

CFJ:	CFIO01_00885 CFIO01_01228 CFIO01_01926 CFIO01_04006 CFIO01_08348

CLUP:

CLUP02_09647 CLUP02_10990 CLUP02_13036 CLUP02_16758

CHIG:

CH63R_08769 CH63R_09712 CH63R_13275

SAPO:

SAPIO_CDS8557 SAPIO_CDS9070

ELA:	UCREL1_10476 UCREL1_1467 UCREL1_1483 UCREL1_7373 UCREL1_764 UCREL1_9722

PFY:	PFICI_02482 PFICI_05027 PFICI_06779 PFICI_08637 PFICI_09039 PFICI_11856

SSL:	SS1G_05151 SS1G_06264 SS1G_07863 SS1G_13051

BFU:	BCIN_01g00640 BCIN_05g06510 BCIN_12g02910 BCIN_15g01170

MBE:	MBM_01462 MBM_01896 MBM_04275 MBM_06962 MBM_09959

PSCO:

LY89DRAFT_266653 LY89DRAFT_739447 LY89DRAFT_742888 LY89DRAFT_780009

GLZ:	GLAREA_00977 GLAREA_03815 GLAREA_05733

ANI:	ANIA_07230

AFM:	AFUA_2G01180 AFUA_2G17620

ACT:	ACLA_076510 ACLA_094490

NFI:	NFIA_033480 NFIA_093020

AOR:	AO090102000058 AO090113000054

ANG:	An02g09270 An10g00390

AFV:	AFLA_009770 AFLA_011511

ALUC:

AKAW2_10793A AKAW2_71039S

ACHE:

ACHE_20113S ACHE_40057A

APUU:

APUU_20182S APUU_71209S

PCS:	N7525_008931

PDP:	PDIP_07720

POU:	POX_a00814

TRG:	TRUGW13939_09239

PNO:	SNOG_02444 SNOG_10188 SNOG_11248 SNOG_13073

PTE:	PTT_04706 PTT_09415 PTT_12135

BZE:	COCCADRAFT_111999 COCCADRAFT_3787 COCCADRAFT_81268

BSC:	COCSADRAFT_196954 COCSADRAFT_199941 COCSADRAFT_34768

BOR:	COCMIDRAFT_2145 COCMIDRAFT_25331 COCMIDRAFT_35852 COCMIDRAFT_91230

AALT:

CC77DRAFT_1010416 CC77DRAFT_950453 CC77DRAFT_959348

ARAB:

EKO05_0006800 EKO05_0007937 EKO05_0009975 EKO05_0010784

ZTR:	MYCGRDRAFT_62587(CDH)

PFJ:	MYCFIDRAFT_215593 MYCFIDRAFT_77759

FFU:	CLAFUR5_06958 CLAFUR5_14150

CBET:

CB0940_09264 CB0940_11021

NPA:	UCRNP2_206 UCRNP2_2863 UCRNP2_3739 UCRNP2_5184 UCRNP2_7189

TML:	GSTUM_00008390001

TVS:	TRAVEDRAFT_73596

DSQ:	DICSQDRAFT_153749

PCO:	PHACADRAFT_259608

SHS:	STEHIDRAFT_62168

HIR:	HETIRDRAFT_157537(cdh1)

PSQ:	PUNSTDRAFT_107198

ADL:	AURDEDRAFT_161830

FME:	FOMMEDRAFT_139496

GTR:	GLOTRDRAFT_113732

RSX:	RhiXN_01644 RhiXN_04270 RhiXN_04278 RhiXN_11843

CCI:	CC1G_09923

ABP:	AGABI1DRAFT107890(AGABI1DRAFT_107890)

ABV:	AGABI2DRAFT188178(AGABI2DRAFT_188178)

MPR:	MPER_11289

MRR:	Moror_16128 Moror_1980

E1B28_007783(CDH1)

SCM:	SCHCO_02642438(SCHCODRAFT_02642438)

CPUT:

CONPUDRAFT_131886 CONPUDRAFT_140809

SLA:	SERLADRAFT_453176(CDH2) SERLADRAFT_491377

PIF:	PITG_00805 PITG_07303 PITG_16169 PITG_18951

PSOJ:

PHYSODRAFT_316871 PHYSODRAFT_346580 PHYSODRAFT_482381 PHYSODRAFT_517891 PHYSODRAFT_557002

SPAR:

SPRG_01483 SPRG_01485 SPRG_01486 SPRG_13203

RHW:	BFN03_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

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

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

DBGET integrated database retrieval system