KEGG   ENZYME: 1.14.99.56
Entry
EC 1.14.99.56               Enzyme                                 

Name
lytic cellulose monooxygenase (C4-dehydrogenating)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
Miscellaneous
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)
R11747
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
NCR: NCU01050(gh61-4)
NTE: NEUTE1DRAFT16830(NEUTE1DRAFT_16830) NEUTE1DRAFT98179(NEUTE1DRAFT_98179)
SMP: SMAC_02729
PAN: PODANSg8289
MTM: MYCTH_100518 MYCTH_55803
CTHR: CTHT_0068920
MGR: MGG_07686 MGG_09709
TMN: UCRPA7_2782
VAL: VDBG_06653
VDA: VDAG_05708
PTE: PTT_19298
HIR: HETIRDRAFT_173373(gh61.7) HETIRDRAFT_58346(GH61E)
SCO: SCO0643(SCF91.03c)
SHY: SHJG_4189
SFA: Sfla_0248
STRP: F750_6768
SPRI: SPRI_6276
SLE: sle_03840(sle_03840) sle_04310(sle_04310)
SLAU: SLA_5870
SGE: DWG14_00994(cbpD_1)
XCE: Xcel_2244
IDO: I598_1144(celB)
CFI: Celf_0270
TFU: Tfu_1268
NDA: Ndas_3518
AMD: AMED_1406 AMED_3114(cpbD)
AMM: AMES_1397 AMES_3080(cpbD)
AMZ: B737_1398 B737_3081(cpbD)
AMYY: YIM_08095 YIM_19840(gbpA3)
AORI: SD37_18685
AHG: AHOG_13415 AHOG_16015(gbpA3)
AFS: AFR_17880
PSUU: Psuf_047550 Psuf_074430(cpbD_2)
 » show all
Reference
1  [PMID:22188218]
  Authors
Beeson WT, Phillips CM, Cate JH, Marletta MA
  Title
Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases.
  Journal
J Am Chem Soc 134:890-2 (2012)
DOI:10.1021/ja210657t
  Sequence
[ncr:NCU01050]
Reference
2  [PMID:22578542]
  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
Structure 20:1051-61 (2012)
DOI:10.1016/j.str.2012.04.002
  Sequence
[ncr:NCU01050]
Reference
3  [PMID:24912171]
  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
Proc Natl Acad Sci U S A 111:8446-51 (2014)
DOI:10.1073/pnas.1402771111
  Sequence
[sco:SCO0643]
Reference
4  [PMID:26178376]
  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
J Biol Chem 290:22955-69 (2015)
DOI:10.1074/jbc.M115.660183
  Sequence
[ncr:NCU02916]
Reference
5  [PMID:27213015]
  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
Biotechnol Biofuels 9:108 (2016)
DOI:10.1186/s13068-016-0520-3
Other DBs
ExplorEnz - The Enzyme Database: 1.14.99.56
IUBMB Enzyme Nomenclature: 1.14.99.56
ExPASy - ENZYME nomenclature database: 1.14.99.56
BRENDA, the Enzyme Database: 1.14.99.56

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