Information on EC 1.14.99.56 - lytic cellulose monooxygenase (C4-dehydrogenating)

for references in articles please use BRENDA:EC1.14.99.56
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.99.56
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RECOMMENDED NAME
GeneOntology No.
lytic cellulose monooxygenase (C4-dehydrogenating)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[(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
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
cellulose, hydrogen-donor:oxygen oxidoreductase (D-glucosyl C4-dehydrogenating)
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)].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-(1->3,1->4)-glucan + ascorbate + O2
C4-oxidized glucan oligosaccharides + dehydroascorbate + H2O
show the reaction diagram
substrate is regenerated amorphous cellulose
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?
cellohexaose + acceptor + O2
oxidized cellobiose and cellotriose + reduced acceptor + H2O
show the reaction diagram
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?
cellotetraose + acceptor + O2
? + reduced acceptor + H2O
show the reaction diagram
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?
cellotriose + acceptor + O2
? + reduced acceptor + H2O
show the reaction diagram
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?
cellulose + ascorbate + O2
C4-oxidized gluco-oligosaccharides + dehydroascorbate + H2O
show the reaction diagram
substrate is regenerated amorphous cellulose
sole release of C4-oxidized and non-oxidized gluco-oligosaccharides
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?
cellulose + dopamine + O2
C4-oxidized gluco-oligosaccharides + 4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O
show the reaction diagram
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dopamine shows 6% of the activity with ascorbate
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?
phosphoric acid swollen cellulose + acceptor + O2
oxidized cellobiose and cellotriose + reduced acceptor + H2O
show the reaction diagram
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main products, C4 is the sole site of oxidation
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?
phosphoric acid swollen cellulose + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
xyloglucan + ascorbate + O2
C4-oxidized oligosaccharides + dehydroascorbate + H2O
show the reaction diagram
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cellobiose
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little product inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.049
Cellotetraose
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pH 7.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11
Cellotetraose
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pH 7.0, 37°C
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
substrate cellohexaose binds to subsites ?4 to +2, and cellotriose from subsites -1 to +2. Residue Tyr203 is placed approximately 15 A away from the copper active site
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comparison of isoforms LPMO9A, LPMO9B and LPMO9C. LPMO9B contains distal from the coordinated copper sphere an additional loop (Gly115-Asn121), which is not present in LPMO9A and LPMO9C. The copper ion in LPMO9A, LPMO9B and LPMO9C is coordinated by His1-His68-Tyr153, His1-His79-Tyr170 and His1-His84-Tyr166, respectively. All three LPMOs share two putative disulfide bridges
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Aspergillus oryzae
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