Entry
Name
lytic cellulose monooxygenase (C4-dehydrogenating)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
Miscellaneous
BRITE hierarchy
Sysname
cellulose, hydrogen-donor:oxygen oxidoreductase (D-glucosyl 4-dehydrogenating)
Reaction(IUBMB)
[(1->4)-beta-D-glucosyl]n+m + reduced acceptor + O2 = 4-dehydro-beta-D-glucosyl-[(1->4)-beta-D-glucosyl]n-1 + [(1->4)-beta-D-glucosyl]m + acceptor + H2O [RN:
R11747 ]
Reaction(KEGG)
Substrate
[(1->4)-beta-D-glucosyl]n+m;
reduced acceptor [CPD:
C00030 ];
O2 [CPD:
C00007 ]
Product
4-dehydro-beta-D-glucosyl-[(1->4)-beta-D-glucosyl]n-1 [CPD:
C21628 ];
[(1->4)-beta-D-glucosyl]m;
acceptor [CPD:
C00028 ];
H2O [CPD:
C00001 ]
Comment
This copper-containing enzyme, found in fungi and bacteria, cleaves cellulose in an oxidative manner. The cellulose fragments that are formed contain a 4-dehydro-D-glucose residue at the non-reducing end. Some enzymes also oxidize cellulose at the C-1 position of the reducing end forming a D-glucono-1,5-lactone residue [cf. EC
1.14.99.54 , lytic cellulose monooxygenase (C1-hydroxylating)].
History
EC 1.14.99.56 created 2017
Orthology
K22032 lytic cellulose monooxygenase (C4-dehydrogenating)
K22033 lytic cellulose monooxygenase (C4-dehydrogenating)
Genes
NTE : NEUTE1DRAFT16830(NEUTE1DRAFT_16830) NEUTE1DRAFT98179(NEUTE1DRAFT_98179)
MTM : MYCTH_100518 MYCTH_55803
PPEI : PpBr36_02492 PpBr36_10121
CFJ : CFIO01_08296 CFIO01_11829
SAPO : SAPIO_CDS0715 SAPIO_CDS2413 SAPIO_CDS5581 SAPIO_CDS8558
AALT : CC77DRAFT_560365 CC77DRAFT_930851
ARAB : EKO05_0003920 EKO05_0009977
TVS : TRAVEDRAFT_36998 TRAVEDRAFT_45192
DSQ : DICSQDRAFT_106787 DICSQDRAFT_108020
HIR : HETIRDRAFT_173373(gh61.7) HETIRDRAFT_58346(GH61E)
SCM : SCHCO_02634027(SCHCODRAFT_02634027)
SRC : M271_17240 M271_39590
SMAL : SMALA_1378 SMALA_5277
SSOI : I1A49_10405 I1A49_30095
SGU : SGLAU_17860 SGLAU_31800 SGLAU_31955
SCW : TU94_28680 TU94_31990
STRC : AA958_22300 AA958_30715
SAMB : SAM23877_2400 SAM23877_6899
SRW : TUE45_01353 TUE45_03305
SLE : sle_03840(sle_03840) sle_04310(sle_04310)
STRD : NI25_01805 NI25_18230
SAUO : BV401_10725 BV401_30210
SAST : CD934_01630 CD934_32860
SNK : CP967_00560 CP967_04595
SHAW : CEB94_02190 CEB94_04840
SPRA : CP972_02775 CP972_30155
SMAO : CAG99_00455 CAG99_05110 CAG99_14445 CAG99_21460
CELZ : E5225_16280 E5225_16290 E5225_17100
CEJ : GC089_17335 GC089_17345 GC089_18000
CIRA : LFM56_16650 LFM56_17160
CDON : KKR89_00820 KKR89_01720
CWAN : KG103_00785 KG103_01815
CXIE : NP048_01015 NP048_01900
THAO : NI17_000695 NI17_006675
TALX : FOF52_00135 FOF52_03340
STRR : EKD16_04575 EKD16_19220
AMD : AMED_1406 AMED_3114(cpbD)
AMM : AMES_1397 AMES_3080(cpbD)
AMZ : B737_1398 B737_3081(cpbD)
AAB : A4R43_03160 A4R43_06485
AMYY : YIM_08095 YIM_19840(gbpA3)
APRT : MUY14_19995 MUY14_20685
APRE : CNX65_12550 CNX65_23370
SSYI : EKG83_12625 EKG83_22020 EKG83_22455 EKG83_28575 EKG83_41375
AHM : TL08_13345 TL08_13515
ACTI : UA75_14350 UA75_18525
ACAD : UA74_14260 UA74_18035
AHG : AHOG_13415 AHOG_16015(gbpA3)
ACTU : Actkin_00625 Actkin_02364 Actkin_03225
UME : RM788_10360 RM788_46605
MAU : Micau_1630 Micau_3953
MICB : MicB006_1654 MicB006_3015
MTUA : CSH63_05960 CSH63_16130
MICH : FJK98_08510 FJK98_21040
MCAB : HXZ27_09425 HXZ27_10185 HXZ27_30320
VMA : VAB18032_09980 VAB18032_12745
MCRA : ID554_04010 ID554_30580
VER : HUT12_08995 HUT12_13925 HUT12_14465
MENO : Jiend_03680 Jiend_11450 Jiend_27360
MCHL : PVK74_10130 PVK74_29370
AMS : AMIS_32650 AMIS_36720
ACTN : L083_3734 L083_4711
ASIC : Q0Z83_034870 Q0Z83_059600
PLAB : C6361_01330 C6361_04905 C6361_07730 C6361_07755 C6361_21720
PLAT : C6W10_01435 C6W10_04320 C6W10_04345 C6W10_16680 C6W10_20320
PFLA : Pflav_032030 Pflav_084660
PSUU : Psuf_047550 Psuf_074430(cpbD_2)
CATI : CS0771_45810 CS0771_70230
GLY : K3N28_06270 K3N28_17545 K3N28_17550
» show all
Taxonomy
Reference
Authors
Beeson WT, Phillips CM, Cate JH, Marletta MA
Title
Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases.
Journal
Sequence
Reference
Authors
Li X, Beeson WT 4th, Phillips CM, Marletta MA, Cate JH
Title
Structural basis for substrate targeting and catalysis by fungal polysaccharide monooxygenases.
Journal
Sequence
Reference
Authors
Forsberg Z, Mackenzie AK, Sorlie M, Rohr AK, Helland R, Arvai AS, Vaaje-Kolstad G, Eijsink VG
Title
Structural and functional characterization of a conserved pair of bacterial cellulose-oxidizing lytic polysaccharide monooxygenases.
Journal
Sequence
Reference
Authors
Borisova AS, Isaksen T, Dimarogona M, Kognole AA, Mathiesen G, Varnai A, Rohr AK, Payne CM, Sorlie M, Sandgren M, Eijsink VG
Title
Structural and Functional Characterization of a Lytic Polysaccharide Monooxygenase with Broad Substrate Specificity.
Journal
Sequence
Reference
Authors
Patel I, Kracher D, Ma S, Garajova S, Haon M, Faulds CB, Berrin JG, Ludwig R, Record E
Title
Salt-responsive lytic polysaccharide monooxygenases from the mangrove fungus Pestalotiopsis sp. NCi6.
Journal
Other DBs