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2,6-dimethoxyphenol + 2 H2O2
coerulignone + 2 H2O
-
-
-
-
?
amorphous cellulose + 2 AH2 + 2 O2
cellooligosaccharide-C6-aldehyde-C1-lactone + 2 A + 2 H2O
amorphous cellulose + AH2 + O2
cellooligosaccharide-C1-lactone + A + H2O
avicel + ascorbate + O2
? + dehydroascorbate + H2O
avicel + ascorbate + O2
C1-oxidized cellooligosaccharides + dehydroascorbate + H2O
avicel + ascorbate + O2
C4-oxidized cellooligosaccharides + C1/C4-oxidized cellooligosaccharides + dehydroascorbate + H2O
avicel + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
-
?
avicel + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
-
?
avicel PH 101 + ascorbic acid + O2
? + dehydroascorbic acid + H2O
bacterial microcrystalline cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
individual AA9A molecules exhibit intermittent random movement along, across, and penetrating into the ribbon-like microfibril structure of bacterial microcrystalline cellulose, concomitant with the release of a small amount of oxidized sugars and the splitting of large cellulose ribbons into fibrils with smaller diameters
-
-
?
beta-(1->3,1->4)-glucan + acceptor + O2
C1/C4-oxidized oxidized glucan oligosaccharides + reduced acceptor + H2O
-
-
-
?
beta-chitin + ascorbate + O2
C4-oxidized oligosaccharides + C1/C4-oxidized oligosaccharides + dehydroascorbate + H2O
birchwood cellulose + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
?
cellohexaosyl-(2-aminobenzamide) + ascorbate + O2
cellotriose + oxidized cellotriosyl-(2-aminobenzamide) + dehydroascorbate + H2O
-
-
-
?
cellooligosaccharide + pyrogallol + O2
?
-
-
-
?
cellulose + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
?
cellulose + ascorbate + O2
C1-oxidized cellooligosaccharides + cellooligosaccharides + dehydroascorbate + H2O
substrate is regenerated amorphous cellulose
release of C1-oxidized and non-oxidized glucooligosaccharides
-
?
cellulose + ascorbate + O2
C1-oxidized cellooligosaccharides + dehydroascorbate + H2O
cellulose + ascorbate + O2
C1/C4-oxidized cellooligosaccharides + cellooligosaccharides + dehydroascorbate + H2O
substrate regenerated amorphous cellulose
enzyme cleaves beta-(1->4)-glucosyl bonds in cellulose under formation of oxidized gluco-oligosaccharides. Both C1 and C4 oxidized gluco-oligosaccharides and non-oxidized gluco-oligosaccharides are formed
-
?
cellulose + ascorbate + O2
C1/C4-oxidized cellooligosaccharides + dehydroascorbate + H2O
cellulose + ascorbic acid + O2
? + dehydroascorbate + H2O
cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
-
?
cellulose + oxidized dopamine + O2
C1-oxidized gluco-oligosaccharides + glucooligosaccharides + dopamine + H2O
-
dopamine shows 46% of the activity with ascorbate
-
?
cellulose + reduced acceptor + O2
? + oxidized acceptor + H2O
-
-
-
-
?
cellulose acetate + ? + O2
? + H2O
-
lytic polysaccharide monooxygenase is able to cleave cellulose acetates with a degree of acetylation of up to 1.4. Preferentially, fragments with a low degree of acetylation are released
-
-
?
chitin + ascorbic acid + O2
? + dehydroascorbate + H2O
filter paper + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
-
?
filter paper + ascorbic acid + O2
? + dehydroascorbic acid + H2O
Kraft pulp + gallate + O2
? + H2O
-
-
-
-
?
microcrystalline cellulose + AH2 + O2
?
-
enzyme catalyzes release of a mixture of soluble sugars comprising reduced and oxidized cellooligosaccharides. The degree of polymerization of the released oligosaccharides ranges from 3 to 5 for the reduced products and from 2 to 5 for the oxidized products
-
?
NaOH pretreated soy spent flakes + ascorbic acid + O2
? + dehydroascorbic acid + H2O
NaOH-treated soy spent flake + ascorbate + O2
C1/C4-oxidized cellooligosaccharides + dehydroascorbate + H2O
-
native soy spentflake is not a substrate
-
?
phosphoric acid swollen cellulase + ascorbic acid + O2
? + dehydroascorbate + H2O
phosphoric acid swollen cellulose + AH2 + O2
? + dehydroascorbate + H2O
phosphoric acid swollen cellulose + ascorbate + O2
C1-oxidized cellooligosaccharides + dehydroascorbate + H2O
phosphoric acid swollen cellulose + ascorbate + O2
C1/C4-oxidized cellooligosaccharides + dehydroascorbate + H2O
-
enzyme oxidizes cellulose at both the C1 and C4 positions
-
?
phosphoric acid swollen cellulose + ascorbate + O2
C4-dehydro-cellooligosaccharide + dehydroascorbate + 2 H2O
KR825269, KR825270
-
The chain lengths of the cellooligosaccharides ranges from 2 to 5
-
?
phosphoric acid swollen cellulose + ascorbate + O2
C4-dehydro-cellooligosaccharide-C1-lactone + dehydroascorbate + H2O
KR825269, KR825270
-
the initially formed lactone at the reducing end of the produced cellooligosaccharides is hydrolyzed spontanously to the aldonic acid. The chain lengths of the cellooligosaccharides ranges from 2 to 5
-
?
phosphoric acid swollen cellulose + ascorbate + O2
cellooligosaccharide-C1-lactone + dehydroascorbate + H2O
KR825269, KR825270
-
the initially formed lactone at the reducing end of the produced cellooligosaccharides is hydrolyzed spontanously to the aldonic acid. The chain lengths of the cellooligosaccharides ranges from 2 to 5
-
?
phosphoric acid swollen cellulose + ascorbate + O2
oxidized cellooligosaccharides + dehydroascorbate + H2O
phosphoric acid swollen cellulose + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
-
?
phosphoric acid swollen cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
phosphoric acid swollen cellulose + ascorbic acid + O2
cellobionic acid + ? + dehydroascorbate + H2O
phosphoric acid-swollen cellulose + ascorbate + O2
cellooligosaccharide + dehydroascorbate + H2O
-
-
-
?
reduced xyloglucan oligosaccharide + ascorbic acid + O2
xyloglucan oligosaccharides + dehydroascorbic acid + H2O
regenerated amorphous cellulose + 3-methylcatechol + O2
3-methyl-o-benzoquinone + H2O
-
-
-
?
regenerated amorphous cellulose + 3-methylcatechol + O2
? + 3-methyl-o-benzoquinone + H2O
-
-
-
?
regenerated amorphous cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
?
regenerated amorphous cellulose + ascorbic acid + O2
dehydroascorbic acid + H2O
-
-
-
?
soluble beta-glucan + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
-
?
steam-exploded spruce + ascorbate + O2
C1-oxidized cellooligosaccharides + dehydroascorbate + H2O
-
-
-
?
tamarind xyloglucan + ascorbic acid + O2
? + dehydroascorbic acid + H2O
xylan + dopamine + O2
C1/C4-oxidized oxidized xylo-oligosaccharides + 4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O
-
93% of the activiy with ascorbate
-
?
xylan + dopamine + O2
C1/C4-oxidized xylooligosaccharides + 4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O
-
enzyme cleaves beta-(1->4)-xylosyl bonds in xylan under formation of oxidized xylo-oligosaccharides
-
?
xyloglucan + acceptor + O2
C1/C4-oxidized oxidized oligosaccharides + reduced acceptor + H2O
-
-
-
?
xyloglucan + ascorbate + O2
?
[(1->4)-beta-D-glucosyl]n+m + AH2 + O2
[(1->4)-beta-D-glucosyl]m-1-(1->4)-D-glucono-1,5-lactone + [(1->4)-beta-D-glucosyl]n + A + H2O
[(1->4)-beta-D-xylosyl]6-(1->4)-beta-D-glucose + ascorbate + O2
?
additional information
?
-
amorphous cellulose + 2 AH2 + 2 O2
cellooligosaccharide-C6-aldehyde-C1-lactone + 2 A + 2 H2O
-
the initially formed lactone at the reducing end of the produced cellooligosaccharides is hydrolyzed spontanously to the aldonic acid. The chain lengths of the cellooligosaccharides ranges from 2 to 5
-
?
amorphous cellulose + 2 AH2 + 2 O2
cellooligosaccharide-C6-aldehyde-C1-lactone + 2 A + 2 H2O
-
the initially formed lactone at the reducing end of the produced cellooligosaccharides is hydrolyzed spontanously to the aldonic acid. The chain lengths of the cellooligosaccharides ranges from 2 to 5
-
?
amorphous cellulose + AH2 + O2
cellooligosaccharide-C1-lactone + A + H2O
-
the initially formed lactone at the reducing end of the produced cellooligosaccharides is hydrolyzed spontanously to the aldonic acid. The chain lengths of the cellooligosaccahdides ranges from 2 to 5
-
?
amorphous cellulose + AH2 + O2
cellooligosaccharide-C1-lactone + A + H2O
-
the initially formed lactone at the reducing end of the produced cellooligosaccharides is hydrolyzed spontanously to the aldonic acid. The chain lengths of the cellooligosaccharides ranges from 2 to 5
-
?
amorphous cellulose + AH2 + O2
cellooligosaccharide-C1-lactone + A + H2O
-
the initially formed lactone at the reducing end of the produced cellooligosaccharides is hydrolyzed spontanously to the aldonic acid. The chain lengths of the cellooligosaccahdides ranges from 2 to 5
-
?
amorphous cellulose + AH2 + O2
cellooligosaccharide-C1-lactone + A + H2O
-
the initially formed lactone at the reducing end of the produced cellooligosaccharides is hydrolyzed spontanously to the aldonic acid. The chain lengths of the cellooligosaccharides ranges from 2 to 5
-
?
avicel + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
?
avicel + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
?
avicel + ascorbate + O2
C1-oxidized cellooligosaccharides + dehydroascorbate + H2O
-
-
-
?
avicel + ascorbate + O2
C1-oxidized cellooligosaccharides + dehydroascorbate + H2O
-
-
-
?
avicel + ascorbate + O2
C4-oxidized cellooligosaccharides + C1/C4-oxidized cellooligosaccharides + dehydroascorbate + H2O
-
-
-
?
avicel + ascorbate + O2
C4-oxidized cellooligosaccharides + C1/C4-oxidized cellooligosaccharides + dehydroascorbate + H2O
-
-
-
?
avicel PH 101 + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
?
avicel PH 101 + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
?
beta-chitin + ascorbate + O2
C4-oxidized oligosaccharides + C1/C4-oxidized oligosaccharides + dehydroascorbate + H2O
substrate squid pen beta-chitin, reaction of EC 1.14.99.53
in addition, considerable amounts of partially deacetylated oligomers are produced
-
?
beta-chitin + ascorbate + O2
C4-oxidized oligosaccharides + C1/C4-oxidized oligosaccharides + dehydroascorbate + H2O
substrate squid pen beta-chitin, reaction of EC 1.14.99.53
in addition, considerable amounts of partially deacetylated oligomers are produced
-
?
cellulose + ascorbate + O2
C1-oxidized cellooligosaccharides + dehydroascorbate + H2O
-
-
-
?
cellulose + ascorbate + O2
C1-oxidized cellooligosaccharides + dehydroascorbate + H2O
-
-
-
?
cellulose + ascorbate + O2
C1/C4-oxidized cellooligosaccharides + dehydroascorbate + H2O
-
-
-
?
cellulose + ascorbate + O2
C1/C4-oxidized cellooligosaccharides + dehydroascorbate + H2O
-
enzyme oxidizes cellulose at both the C1 and C4 positions
-
?
cellulose + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
?
cellulose + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
?
cellulose + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
?
chitin + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
?
chitin + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
?
chitin + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
?
chitin + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
?
filter paper + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
-
?
filter paper + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
-
?
NaOH pretreated soy spent flakes + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
-
?
NaOH pretreated soy spent flakes + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
?
NaOH pretreated soy spent flakes + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
-
?
phosphoric acid swollen cellulase + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
?
phosphoric acid swollen cellulase + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
?
phosphoric acid swollen cellulase + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
?
phosphoric acid swollen cellulase + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
?
phosphoric acid swollen cellulose + AH2 + O2
? + dehydroascorbate + H2O
-
in presence of cellobiose dehydrogenase, products include doubly oxidized cellodextrin
-
?
phosphoric acid swollen cellulose + AH2 + O2
? + dehydroascorbate + H2O
-
in presence of cellobiose dehydrogenase, products include doubly oxidized cellodextrin
-
?
phosphoric acid swollen cellulose + ascorbate + O2
C1-oxidized cellooligosaccharides + dehydroascorbate + H2O
-
-
-
?
phosphoric acid swollen cellulose + ascorbate + O2
C1-oxidized cellooligosaccharides + dehydroascorbate + H2O
-
-
-
?
phosphoric acid swollen cellulose + ascorbate + O2
C1-oxidized cellooligosaccharides + dehydroascorbate + H2O
-
-
-
?
phosphoric acid swollen cellulose + ascorbate + O2
oxidized cellooligosaccharides + dehydroascorbate + H2O
-
-
-
?
phosphoric acid swollen cellulose + ascorbate + O2
oxidized cellooligosaccharides + dehydroascorbate + H2O
-
-
-
?
phosphoric acid swollen cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
-
?
phosphoric acid swollen cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
?
phosphoric acid swollen cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
?
phosphoric acid swollen cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
-
?
phosphoric acid swollen cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
?
phosphoric acid swollen cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
?
phosphoric acid swollen cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
?
phosphoric acid swollen cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
?
phosphoric acid swollen cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
-
?
phosphoric acid swollen cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
?
phosphoric acid swollen cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
?
phosphoric acid swollen cellulose + ascorbic acid + O2
cellobionic acid + ? + dehydroascorbate + H2O
-
-
-
?
phosphoric acid swollen cellulose + ascorbic acid + O2
cellobionic acid + ? + dehydroascorbate + H2O
-
-
-
?
reduced xyloglucan oligosaccharide + ascorbic acid + O2
xyloglucan oligosaccharides + dehydroascorbic acid + H2O
pure xyloglucan oligosaccharide with DP14
-
-
?
reduced xyloglucan oligosaccharide + ascorbic acid + O2
xyloglucan oligosaccharides + dehydroascorbic acid + H2O
pure xyloglucan oligosaccharide with DP14
-
-
?
tamarind xyloglucan + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
?
tamarind xyloglucan + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
?
xyloglucan + ascorbate + O2
?
-
-
-
?
xyloglucan + ascorbate + O2
?
-
-
-
?
[(1->4)-beta-D-glucosyl]n+m + AH2 + O2
[(1->4)-beta-D-glucosyl]m-1-(1->4)-D-glucono-1,5-lactone + [(1->4)-beta-D-glucosyl]n + A + H2O
-
-
-
?
[(1->4)-beta-D-glucosyl]n+m + AH2 + O2
[(1->4)-beta-D-glucosyl]m-1-(1->4)-D-glucono-1,5-lactone + [(1->4)-beta-D-glucosyl]n + A + H2O
-
-
-
?
[(1->4)-beta-D-xylosyl]6-(1->4)-beta-D-glucose + ascorbate + O2
?
-
-
-
?
[(1->4)-beta-D-xylosyl]6-(1->4)-beta-D-glucose + ascorbate + O2
?
-
-
-
?
additional information
?
-
no substrate: xylan, starch, laminarin, chitin. cleavage of cleavage of hemicelluloses and phosphoric acid swollen cellulose C uses both C1- and C4-oxidizing mechanisms, reaction of EC 1.14.99.54 and EC 1.14.99.56
-
-
?
additional information
?
-
enzyme is a family AA13 protein acting on alpha-linked glycosidic bonds
-
-
?
additional information
?
-
-
enzyme is a family AA13 protein acting on alpha-linked glycosidic bonds
-
-
?
additional information
?
-
enzyme is a family AA13 protein acting on alpha-linked glycosidic bonds
-
-
?
additional information
?
-
enzyme catalyzes mixed C1/C4 oxidative cleavage of cellulose, reactions of EC 1.14.99.54 and EC1.14.99.56, and xyloglucan, reaction of lytic xyloglucan monooxygenase, but is inactive toward other (1,4)-linked beta-glucans or chitin and cellooligosaccharides with a degree of polymerization DP 3-6. It shows broad specificity on xyloglucan, cleaving any glycosidic bond in the beta-glucan main chain, regardless of xylosyl substitutions. When incubated with a mixture of xyloglucan and cellulose, LPMO9A efficiently attacks the xyloglucan, whereas cellulose conversion is inhibited. no substrates: xyloglucan-heptamer, birchwood xylan, wheat arabinoxylan, konjac glucomannan, ivory nut mannan, beta-glucan from barley, lichenan from Icelandic moss, starch, and spruce galactoglucomannan
-
-
?
additional information
?
-
enzyme catalyzes mixed C1/C4 oxidative cleavage of cellulose, reactions of EC 1.14.99.54 and EC1.14.99.56, and xyloglucan, reaction of lytic xyloglucan monooxygenase, but is inactive toward other (1,4)-linked beta-glucans or chitin and cellooligosaccharides with a degree of polymerization DP 3-6. It shows broad specificity on xyloglucan, cleaving any glycosidic bond in the beta-glucan main chain, regardless of xylosyl substitutions. When incubated with a mixture of xyloglucan and cellulose, LPMO9A efficiently attacks the xyloglucan, whereas cellulose conversion is inhibited. no substrates: xyloglucan-heptamer, birchwood xylan, wheat arabinoxylan, konjac glucomannan, ivory nut mannan, beta-glucan from barley, lichenan from Icelandic moss, starch, and spruce galactoglucomannan
-
-
?
additional information
?
-
-
no substrate: carboxymethylcellulose or short cellooligosaccharides
-
-
?
additional information
?
-
mechanism may follow one electron reduction of PMO-Cu(II) to PMO-Cu(I) by the cellobiose dehydrogenase heme domain followed by oxygen binding and internal electron transfer to form a copper superoxo intermediate. Hydrogen atom abstraction by the copper superoxo at the 1-position of an internal carbohydrate then takes place, generating a copper hydroperoxo intermediate and a substrate radical. The second electron from cellobiose dehydrogenase then facilitates O-O bond cleavage releasing water and generating a copper oxo radical that couples with the substrate radical, thereby hydroxylating the polysaccharide. The additional oxygen atom destabilizes the glycosidic bond leading to elimination of the adjacent glucan and formation of a sugar lactone or ketoaldose
-
-
?
additional information
?
-
mechanism may follow one electron reduction of PMO-Cu(II) to PMO-Cu(I) by the cellobiose dehydrogenase heme domain followed by oxygen binding and internal electron transfer to form a copper superoxo intermediate. Hydrogen atom abstraction by the copper superoxo at the 1-position of an internal carbohydrate then takes place, generating a copper hydroperoxo intermediate and a substrate radical. The second electron from cellobiose dehydrogenase then facilitates O-O bond cleavage releasing water and generating a copper oxo radical that couples with the substrate radical, thereby hydroxylating the polysaccharide. The additional oxygen atom destabilizes the glycosidic bond leading to elimination of the adjacent glucan and formation of a sugar lactone or ketoaldose
-
-
?
additional information
?
-
mechanism may follow one electron reduction of PMO-Cu(II) to PMO-Cu(I) by the cellobiose dehydrogenase heme domain followed by oxygen binding and internal electron transfer to form a copper superoxo intermediate. Hydrogen atom abstraction by the copper superoxo at the 1-position of an internal carbohydrate then takes place, generating a copper hydroperoxo intermediate and a substrate radical. The second electron from cellobiose dehydrogenase then facilitates O-O bond cleavage releasing water and generating a copper oxo radical that couples with the substrate radical, thereby hydroxylating the polysaccharide. The additional oxygen atom destabilizes the glycosidic bond leading to elimination of the adjacent glucan and formation of a sugar lactone or ketoaldose
-
-
?
additional information
?
-
mechanism may follow one electron reduction of PMO-Cu(II) to PMO-Cu(I) by the cellobiose dehydrogenase heme domain followed by oxygen binding and internal electron transfer to form a copper superoxo intermediate. Hydrogen atom abstraction by the copper superoxo at the 4-position of an internal carbohydrate then takes place, generating a copper hydroperoxo intermediate and a substrate radical. The second electron from cellobiose dehydrogenase then facilitates O-O bond cleavage releasing water and generating a copper oxo radical that couples with the substrate radical, thereby hydroxylating the polysaccharide. The additional oxygen atom destabilizes the glycosidic bond leading to elimination of the adjacent glucan and formation of a sugar lactone or ketoaldose
-
-
?
additional information
?
-
mechanism may follow one electron reduction of PMO-Cu(II) to PMO-Cu(I) by the cellobiose dehydrogenase heme domain followed by oxygen binding and internal electron transfer to form a copper superoxo intermediate. Hydrogen atom abstraction by the copper superoxo at the 4-position of an internal carbohydrate then takes place, generating a copper hydroperoxo intermediate and a substrate radical. The second electron from cellobiose dehydrogenase then facilitates O-O bond cleavage releasing water and generating a copper oxo radical that couples with the substrate radical, thereby hydroxylating the polysaccharide. The additional oxygen atom destabilizes the glycosidic bond leading to elimination of the adjacent glucan and formation of a sugar lactone or ketoaldose
-
-
?
additional information
?
-
mechanism may follow one electron reduction of PMO-Cu(II) to PMO-Cu(I) by the cellobiose dehydrogenase heme domain followed by oxygen binding and internal electron transfer to form a copper superoxo intermediate. Hydrogen atom abstraction by the copper superoxo at the 4-position of an internal carbohydrate then takes place, generating a copper hydroperoxo intermediate and a substrate radical. The second electron from cellobiose dehydrogenase then facilitates O-O bond cleavage releasing water and generating a copper oxo radical that couples with the substrate radical, thereby hydroxylating the polysaccharide. The additional oxygen atom destabilizes the glycosidic bond leading to elimination of the adjacent glucan and formation of a sugar lactone or ketoaldose
-
-
?
additional information
?
-
mechanism may follow one electron reduction of PMO-Cu(II) to PMO-Cu(I) by the cellobiose dehydrogenase heme domain followed by oxygen binding and internal electron transfer to form a copper superoxo intermediate. Hydrogen atom abstraction by the copper superoxo at the 4-position of an internal carbohydrate then takes place, generating a copper hydroperoxo intermediate and a substrate radical. The second electron from cellobiose dehydrogenase then facilitates O-O bond cleavage releasing water and generating a copper oxo radical that couples with the substrate radical, thereby hydroxylating the polysaccharide. The additional oxygen atom destabilizes the glycosidic bond leading to elimination of the adjacent glucan and formation of a sugar lactone or ketoaldose
-
-
?
additional information
?
-
mechanism may follow one electron reduction of PMO-Cu(II) to PMO-Cu(I) by the cellobiose dehydrogenase heme domain followed by oxygen binding and internal electron transfer to form a copper superoxo intermediate. Hydrogen atom abstraction by the copper superoxo at the 4-position of an internal carbohydrate then takes place, generating a copper hydroperoxo intermediate and a substrate radical. The second electron from cellobiose dehydrogenase then facilitates O-O bond cleavage releasing water and generating a copper oxo radical that couples with the substrate radical, thereby hydroxylating the polysaccharide. The additional oxygen atom destabilizes the glycosidic bond leading to elimination of the adjacent glucan and formation of a sugar lactone or ketoaldose
-
-
?
additional information
?
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mechanism may follow one electron reduction of PMO-Cu(II) to PMO-Cu(I) by the cellobiose dehydrogenase heme domain followed by oxygen binding and internal electron transfer to form a copper superoxo intermediate. Hydrogen atom abstraction by the copper superoxo at the 4-position of an internal carbohydrate then takes place, generating a copper hydroperoxo intermediate and a substrate radical. The second electron from cellobiose dehydrogenase then facilitates O-O bond cleavage releasing water and generating a copper oxo radical that couples with the substrate radical, thereby hydroxylating the polysaccharide. The additional oxygen atom destabilizes the glycosidic bond leading to elimination of the adjacent glucan and formation of a sugar lactone or ketoaldose
-
-
?
additional information
?
-
mechanism may follow one electron reduction of PMO-Cu(II) to PMO-Cu(I) by the cellobiose dehydrogenase heme domain followed by oxygen binding and internal electron transfer to form a copper superoxo intermediate. Hydrogen atom abstraction by the copper superoxo at the 1-position of an internal carbohydrate then takes place, generating a copper hydroperoxo intermediate and a substrate radical. The second electron from cellobiose dehydrogenase then facilitates O-O bond cleavage releasing water and generating a copper oxo radical that couples with the substrate radical, thereby hydroxylating the polysaccharide. The additional oxygen atom destabilizes the glycosidic bond leading to elimination of the adjacent glucan and formation of a sugar lactone or ketoaldose
-
-
?
additional information
?
-
mechanism may follow one electron reduction of PMO-Cu(II) to PMO-Cu(I) by the cellobiose dehydrogenase heme domain followed by oxygen binding and internal electron transfer to form a copper superoxo intermediate. Hydrogen atom abstraction by the copper superoxo at the 1-position of an internal carbohydrate then takes place, generating a copper hydroperoxo intermediate and a substrate radical. The second electron from cellobiose dehydrogenase then facilitates O-O bond cleavage releasing water and generating a copper oxo radical that couples with the substrate radical, thereby hydroxylating the polysaccharide. The additional oxygen atom destabilizes the glycosidic bond leading to elimination of the adjacent glucan and formation of a sugar lactone or ketoaldose
-
-
?
additional information
?
-
mechanism may follow one electron reduction of PMO-Cu(II) to PMO-Cu(I) by the cellobiose dehydrogenase heme domain followed by oxygen binding and internal electron transfer to form a copper superoxo intermediate. Hydrogen atom abstraction by the copper superoxo at the 1-position of an internal carbohydrate then takes place, generating a copper hydroperoxo intermediate and a substrate radical. The second electron from cellobiose dehydrogenase then facilitates O-O bond cleavage releasing water and generating a copper oxo radical that couples with the substrate radical, thereby hydroxylating the polysaccharide. The additional oxygen atom destabilizes the glycosidic bond leading to elimination of the adjacent glucan and formation of a sugar lactone or ketoaldose
-
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?
additional information
?
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enzyme cleaves cellulose, xyloglucan, reaction of lytic xyloglucan monooxogenase, mixed-linkage glucan and glucomannan. Oligosaccharides are cleaved using a C4-oxidizing mechanism, reaction of EC 1.14.99.56, whereas polysaccharides are cleaved with both C1- and C4-oxidizing mechanisms in varying proportions, reactions of EC 1.14.99.54 and EC 1.14.99.56
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?
additional information
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enzyme cleaves cellulose, xyloglucan, reaction of lytic xyloglucan monooxogenase, mixed-linkage glucan and glucomannan. Oligosaccharides are cleaved using a C4-oxidizing mechanism, reaction of EC 1.14.99.56, whereas polysaccharides are cleaved with both C1- and C4-oxidizing mechanisms in varying proportions, reactions of EC 1.14.99.54 and EC 1.14.99.56
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?
additional information
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products are oxidized cellooligosaccharides with DP of 4-8. No substrate: beta-chitin
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?
additional information
?
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isoform CelS2 produces C1-oxidized cellooligosaccharides only
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?
additional information
?
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isoform CelS2 produces C1-oxidized cellooligosaccharides only
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?
additional information
?
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isoform CelS2 produces C1-oxidized cellooligosaccharides only
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?
additional information
?
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isoform CelS2 produces C1-oxidized cellooligosaccharides only
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?
additional information
?
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quantum mechanical calculations predict that oxygen binds end-on to copper, and that a copperoxyl-mediated, oxygen-rebound mechanism is energetically preferred. The N-terminal histidine methylation has only a minor effect on the LPMO active site structure or reactivity for the examined steps
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additional information
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The enzyme also oxidizes wheat arabinoxylan, birchwood glucuronoxylan and oat spelt xylan if assayed in the presence of amorphous cellulose. The enzyme uses cellulose to bind while oxidizing neighboring xylan chains. No activity is observed with wheat arabinoxylan, birchwood glucuronoxylan and oat spelt xylan alone
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?
additional information
?
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-
The enzyme also oxidizes wheat arabinoxylan, birchwood glucuronoxylan and oat spelt xylan if assayed in the presence of amorphous cellulose. The enzyme uses cellulose to bind while oxidizing neighboring xylan chains. No activity is observed with wheat arabinoxylan, birchwood glucuronoxylan and oat spelt xylan alone
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?
additional information
?
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for isoforms LPMO9A, LPMO9B and LPMO9C, ascorbic acid is one of the best electron donors. Besides ascorbic acid, compounds bearing a 1,2-benzenediol moiety such as 3-methylcatechol, 3,4-dihydroxyphenylalanine, or a 1,2,3-benzenetriol moiety such as gallic acid, epigallocatechin-gallate give the highest formation of oxidized and non-oxidized gluco-oligosaccharides. Sinapic acid actes as donor. No electron donor: quercetin or taxifolin, and tannic acid
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-
?
additional information
?
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for isoforms LPMO9A, LPMO9B and LPMO9C, ascorbic acid is one of the best electron donors. Besides ascorbic acid, compounds bearing a 1,2-benzenediol moiety such as 3-methylcatechol, 3,4-dihydroxyphenylalanine, or a 1,2,3-benzenetriol moiety such as gallic acid, epigallocatechin-gallate give the highest formation of oxidized and non-oxidized gluco-oligosaccharides. Sinapic acid actes as donor. No electron donor: quercetin or taxifolin, and tannic acid
-
-
?
additional information
?
-
no substrate: beta-(1->3, 1->4)-glucan. For isoforms LPMO9A, LPMO9B and LPMO9C, ascorbic acid is one of the best electron donors. Besides ascorbic acid, compounds bearing a 1,2-benzenediol moiety such as 3-methylcatechol, 3,4-dihydroxyphenylalanine, or a 1,2,3-benzenetriol moiety such as gallic acid, epigallocatechin-gallate give the highest formation of oxidized and non-oxidized gluco-oligosaccharides. Sinapic acid actes as donor. No electron donor: quercetin or taxifolin, and tannic acid
-
-
?
additional information
?
-
no substrate: beta-(1->3, 1->4)-glucan. For isoforms LPMO9A, LPMO9B and LPMO9C, ascorbic acid is one of the best electron donors. Besides ascorbic acid, compounds bearing a 1,2-benzenediol moiety such as 3-methylcatechol, 3,4-dihydroxyphenylalanine, or a 1,2,3-benzenetriol moiety such as gallic acid, epigallocatechin-gallate give the highest formation of oxidized and non-oxidized gluco-oligosaccharides. Sinapic acid actes as donor. No electron donor: quercetin or taxifolin, and tannic acid
-
-
?
additional information
?
-
The enzyme also oxidizes wheat arabinoxylan, birchwood glucuronoxylan and oat spelt xylan if assayed in the presence of amorphous cellulose. The enzyme uses cellulose to bind while oxidizing neighboring xylan chains. No activity is observed with wheat arabinoxylan, birchwood glucuronoxylan and oat spelt xylan alone
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?
additional information
?
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enzyme acts on xylans bound to cellulos, and the enzyme is able to produce hydrogen peroxide in the presence of ascorbate, cysteine or gallate as electron donors
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?
additional information
?
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enzyme acts on xylans bound to cellulos, and the enzyme is able to produce hydrogen peroxide in the presence of ascorbate, cysteine or gallate as electron donors
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?
additional information
?
-
enzyme acts on xylans bound to cellulose, and the enzyme is able to produce hydrogen peroxide in the presence of ascorbate, cysteine or gallate as electron donors
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?
additional information
?
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enzyme acts on xylans bound to cellulose, and the enzyme is able to produce hydrogen peroxide in the presence of ascorbate, cysteine or gallate as electron donors
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?
additional information
?
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no substrates: galactan, cellopentaose, or cellohexaose with or without the addition of ascorbic acid. Poor substrate: Avicel
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?
additional information
?
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-
no substrates: galactan, cellopentaose, or cellohexaose with or without the addition of ascorbic acid. Poor substrate: Avicel
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?
additional information
?
-
no substrates: galactan, cellopentaose, or cellohexaose
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?
additional information
?
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-
no substrates: galactan, cellopentaose, or cellohexaose
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?
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Bey, M.; Zhou, S.; Poidevin, L.; Henrissat, B.; Coutinho, P.M.; Berrin, J.G.; Sigoillot, J.C.
Cello-oligosaccharide oxidation reveals differences between two lytic polysaccharide monooxygenases (family GH61) from Podospora anserina
Appl. Environ. Microbiol.
79
488-496
2013
Podospora anserina (B2AVF1), Podospora anserina (B2B629), Podospora anserina, Podospora anserina DSM 980 (B2AVF1), Podospora anserina DSM 980 (B2B629)
brenda
Frommhagen, M; Sforza, S.; Westphal, A.H.; Visser, J.; Hinz, S.W.; Koetsier, M.J.; van Berkel, W.J.; Gruppen, H.; Kabel, M.A.
Discovery of the combined oxidative cleavage of plant xylan and cellulose by a new fungal polysaccharide monooxygenase
Biotechnol. Biofuels
17
101
2015
Thermothelomyces thermophilus (A0A0H4K9X4), Thermothelomyces thermophilus, Thermothelomyces thermophilus C1 (A0A0H4K9X4)
brenda
Patel, I.; Kracher, D.; Ma, S.; Garajova, S.; Haon, M.; Faulds, C.B.; Berrin, J.G.; Ludwig, R.; Record, E.
Salt-responsive lytic polysaccharide monooxygenases from the mangrove fungus Pestalotiopsis sp. NCi6
Biotechnol. Biofuels
9
108
2016
Pestalotiopsis sp. NCi6 (KR825269), Pestalotiopsis sp. NCi6 (KR825270)
brenda
Borisova, A.S.; Isaksen, T.; Dimarogona, M.; Kognole; A.A.; Mathiesen, G.; Varnai, A.; Rohr, A.K.; Payne, C.M.; Sorlie, M.; Sandgren, M.; Eijsink, V.G.
Structural and functional characterization of a lytic polysaccharide monooxygenase with broad substrate specificity
J. Biol. Chem.
290
22955-22969
2015
Neurospora crassa (Q7SHI8), Neurospora crassa, Neurospora crassa DSM 1257 (Q7SHI8)
brenda
Arfi, Y.; Shamshoum, M.; Rogachev, I.; Peleg, Y.; Bayer, E.A.
Integration of bacterial lytic polysaccharide monooxygenases into designer cellulosomes promotes enhanced cellulose degradation
Proc. Natl. Acad. Sci. USA
111
9109-9114
2014
Thermobifida fusca (Q47PB9), Thermobifida fusca (Q47QG3)
brenda
Phillips, C.; Beeson, W.; Cate, J.; Marletta, M.
Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa
ACS Chem. Biol.
6
1399-1406
2011
Neurospora crassa (Q1K8B6), Neurospora crassa (Q7RWN7), Neurospora crassa (Q7SA19), Neurospora crassa ATCC 24698 (Q1K8B6), Neurospora crassa ATCC 24698 (Q7RWN7), Neurospora crassa ATCC 24698 (Q7SA19)
brenda
Frandsen, K.; Poulsen, J.; Tovborg, M.; Johansen, K.; Lo Leggio, L.
Learning from oligosaccharide soaks of crystals of an AA13 lytic polysaccharide monooxygenase: Crystal packing, ligand binding and active-site disorder
Acta Crystallogr. Sect. D
73
64-76
2017
Aspergillus oryzae (Q2U8Y3), Aspergillus oryzae, Aspergillus oryzae ATCC 42149 (Q2U8Y3)
brenda
O'Dell, W.; Swartz, P.; Weiss, K.; Meilleur, F.
Crystallization of a fungal lytic polysaccharide monooxygenase expressed from glycoengineered Pichia pastoris for X-ray and neutron diffraction
Acta Crystallogr. Sect. F
73
70-78
2017
Neurospora crassa (Q1K8B6), Neurospora crassa, Neurospora crassa DSM 1257 (Q1K8B6)
brenda
ODell, W.B.; Agarwal, P.K.; Meilleur, F.
Oxygen activation at the active site of a fungal lytic polysaccharide monooxygenase
Angew. Chem. Int. Ed. Engl.
56
767-770
2017
Neurospora crassa (Q1K8B6), Neurospora crassa, Neurospora crassa DSM 1257 (Q1K8B6)
brenda
Book, A.; Yennamalli, R.; Takasuka, T.; Currie, C.; Phillips, G.; Fox, B.
Evolution of substrate specificity in bacterial AA10 lytic polysaccharide monooxygenases
Biotechnol. Biofuels
7
109
2014
Trichoderma reesei, Thermothielavioides terrestris (D0VWZ9), Thermoascus aurantiacus (G3XAP7), Serratia marcescens (O83009), Neurospora crassa (Q1K8B6), Neurospora crassa (Q7SA19), Vibrio cholerae O1 (Q9KLD5), Vibrio cholerae O1 ATCC 39315 (Q9KLD5), Neurospora crassa DSM 1257 (Q1K8B6), Neurospora crassa DSM 1257 (Q7SA19), Trichoderma reesei QM6a
brenda
Frommhagen, M.; Sforza, S.; Westphal, A.; Visser, J.; Hinz, S.; Koetsier, M.; Van Berkel, W.; Gruppen, H.; Kabel, M.
Discovery of the combined oxidative cleavage of plant xylan and cellulose by a new fungal polysaccharide monooxygenase
Biotechnol. Biofuels
8
101
2015
Thermothelomyces thermophilus (A0A0H4K9X4), Thermothelomyces thermophilus
brenda
Frommhagen, M.; Koetsier, M.J.; Westphal, A.H.; Visser, J.; Hinz, S.W.; Vincken, J.P.; van Berkel, W.J.; Kabel, M.A.; Gruppen, H.
Lytic polysaccharide monooxygenases from Myceliophthora thermophila C1 differ in substrate preference and reducing agent specificity
Biotechnol. Biofuels
9
186
2016
Thermothelomyces thermophilus (A0A0H4K9X4), Thermothelomyces thermophilus (A0A1C9CXI1)
brenda
Frandsen, K.E.; Poulsen, J.N.; Tandrup, T.; Lo Leggio, L.
Unliganded and substrate bound structures of the cellooligosaccharide active lytic polysaccharide monooxygenase LsAA9A at low pH
Carbohydr. Res.
448
187-190
2017
Panus similis (A0A0S2GKZ1), Panus similis
brenda
Selig, M.; Vuong, T.; Gudmundsson, M.; Forsberg, Z.; Westereng, B.; Felby, C.; Master, E.
Modified cellobiohydrolase-cellulose interactions following treatment with lytic polysaccharide monooxygenase CelS2 (ScLPMO10C) observed by QCM-D
Cellulose
22
2263-2270
2015
Streptomyces coelicolor (V5N5H9), Streptomyces coelicolor ATCC BAA-471 (V5N5H9)
-
brenda
Pierce, B.C.; Agger, J.W.; Wichmann, J.; Meyer, A.S.
Oxidative cleavage and hydrolytic boosting of cellulose in soybean spent flakes by Trichoderma reesei Cel61A lytic polysaccharide monooxygenase
Enzyme Microb. Technol.
98
58-66
2017
Trichoderma reesei (O14405), Trichoderma reesei
brenda
Wu, M.; Beckham, G.T.; Larsson, A.M.; Ishida, T.; Kim, S.; Payne, C.M.; Himmel, M.E.; Crowley, M.F.; Horn, S.J.; Westereng, B.; Igarashi, K.; Samejima, M.; Stahlberg, J.; Eijsink, V.G.; Sandgren, M.
Crystal structure and computational characterization of the lytic polysaccharide monooxygenase GH61D from the Basidiomycota fungus Phanerochaete chrysosporium
J. Biol. Chem.
288
12828-12839
2013
Phanerodontia chrysosporium (H1AE14), Phanerodontia chrysosporium
brenda
Eibinger, M.; Ganner, T.; Bubner, P.; Rosker, S.; Kracher, D.; Haltrich, D.; Ludwig, R.; Plank, H.; Nidetzky, B.
Cellulose surface degradation by a lytic polysaccharide monooxygenase and its effect on cellulase hydrolytic efficiency
J. Biol. Chem.
289
35929-35938
2014
Neurospora crassa (Q1K4Q1), Neurospora crassa DSM 1257 (Q1K4Q1)
brenda
Vermaas, J.V.; Crowley, M.F.; Beckham, G.T.; Payne, C.M.
Effects of lytic polysaccharide monooxygenase oxidation on cellulose structure and binding of oxidized cellulose oligomers to cellulases
J. Phys. Chem. B
119
6129-6143
2015
Trichoderma reesei (G0RVK1), Trichoderma reesei, Trichoderma reesei QM6a (G0RVK1)
brenda
Kim, S.; Stahlberg, J.; Sandgren, M.; Paton, R.S.; Beckham, G.T.
Quantum mechanical calculations suggest that lytic polysaccharide monooxygenases use a copper-oxyl, oxygen-rebound mechanism
Proc. Natl. Acad. Sci. USA
111
149-154
2014
Thermoascus aurantiacus (G3XAP7)
brenda
Forsberg, Z.; Mackenzie, A.; Sorlie, M.; Rohr, A.; Helland, R.; Arvai, A.; Vaaje-Kolstad, G.; Eijsink, V.
Structural and functional characterization of a conserved pair of bacterial cellulose-oxidizing lytic polysaccharide monooxygenases
Proc. Natl. Acad. Sci. USA
111
8446-8451
2014
Streptomyces coelicolor (Q9RJC1), Streptomyces coelicolor (Q9RJY2), Streptomyces coelicolor ATCC BAA-471 (Q9RJC1), Streptomyces coelicolor ATCC BAA-471 (Q9RJY2)
brenda
Tanghe, M.; Danneels, B.; Last, M.; Beerens, K.; Stals, I.; Desmet, T.
Disulfide bridges as essential elements for the thermostability of lytic polysaccharide monooxygenase LPMO10C from Streptomyces coelicolor
Protein Eng. Des. Sel.
30
401-408
2017
Streptomyces coelicolor (Q9RJY2), Streptomyces coelicolor, Streptomyces coelicolor ATCC BAA-471 (Q9RJY2)
brenda
Li, X.; Beeson IV, W.; Phillips, C.; Marletta, M.; Cate, J.
Structural basis for substrate targeting and catalysis by fungal polysaccharide monooxygenases
Structure
20
1051-1061
2012
Neurospora crassa (Q1K8B6), Neurospora crassa (Q7SA19), Neurospora crassa, Neurospora crassa DSM 1257 (Q1K8B6), Neurospora crassa DSM 1257 (Q7SA19)
brenda
Hedegard, E.; Ryde, U.
Multiscale modelling of lytic polysaccharide monooxygenases
ACS Omega
2
536-545
2017
Thermoascus aurantiacus (G3XAP7)
-
brenda
Frommhagen, M.; Westphal, A.; Hilgers, R.; Koetsier, M.; Hinz, S.; Visser, J.; Gruppen, H.; van Berkel, W.; Kabel, M.
Quantification of the catalytic performance of C1-cellulose-specific lytic polysaccharide monooxygenases
Appl. Microbiol. Biotechnol.
102
1281-1295
2018
Thermothelomyces thermophilus (A0A1C9CXI1), Thermothelomyces heterothallicus (A0A218MJF1)
brenda
Courtade, G.; Forsberg, Z.; Vaaje-Kolstad, G.; Eijsink, V.; Aachmann, F.
Chemical shift assignments for the apo-form of the catalytic domain, the linker region, and the carbohydrate-binding domain of the cellulose-active lytic polysaccharide monooxygenase ScLPMO10C
Biomol. NMR Assign.
11
257-264
2017
Streptomyces coelicolor (Q9RJY2), Streptomyces coelicolor, Streptomyces coelicolor ATCC BAA-471 (Q9RJY2)
brenda
Song, B.; Li, B.; Wang, X.; Shen, W.; Park, S.; Collings, C.; Feng, A.; Smith, S.; Walton, J.; Ding, S.
Real-time imaging reveals that lytic polysaccharide monooxygenase promotes cellulase activity by increasing cellulose accessibility
Biotechnol. Biofuels
11
41
2018
Trichoderma reesei (O14405)
brenda
Breslmayr, E.; Hanzek, M.; Hanrahan, A.; Leitner, C.; Kittl, R.; Santek, B.; Oostenbrink, C.; Ludwig, R.
A fast and sensitive activity assay for lytic polysaccharide monooxygenase
Biotechnol. Biofuels
11
79
2018
Neurospora crassa
brenda
Rodrigues, K.; Macedo, J.; Teixeira, T.; Barros, J.; Araujo, A.; Santos, F.; Quirino, B.; Brasil, B.; Salum, T.; Abdelnur, P.; Favaro, L.
Recombinant expression of Thermobifida fusca E7 LPMO in Pichia pastoris and Escherichia coli and their functional characterization
Carbohydr. Res.
448
175-181
2017
Thermobifida fusca (Q47QG3), Thermobifida fusca E7 (Q47QG3)
brenda
Moellers, K.; Mikkelsen, H.; Simonsen, T.; Cannella, D.; Johansen, K.; Bjerrum, M.; Felby, C.
On the formation and role of reactive oxygen species in light-driven LPMO oxidation of phosphoric acid swollen cellulose
Carbohydr. Res.
448
182-186
2017
Thermoascus aurantiacus, Thermothielavioides terrestris (D0VWZ9)
brenda
Valenzuela, S.; Ferreres, G.; Margalef, G.; Pastor, F.
Fast purification method of functional LPMOs from Streptomyces ambofaciens by affinity adsorption
Carbohydr. Res.
448
205-211
2017
Streptomyces ambofaciens
brenda
Courtade, G.; Le, S.; Satrom, G.; Brautaset, T.; Aachmann, F.
A novel expression system for lytic polysaccharide monooxygenases
Carbohydr. Res.
448
212-219
2017
Bacillus licheniformis, Cellvibrio japonicus
brenda
Pierce, B.; Agger, J.; Zhang, Z.; Wichmann, J.; Meyer, A.
A comparative study on the activity of fungal lytic polysaccharide monooxygenases for the depolymerization of cellulose in soybean spent flakes
Carbohydr. Res.
449
85-94
2017
Aspergillus terreus, Trichoderma reesei (O14405), Trichoderma reesei
brenda
Gusakov, A.; Bulakhov, A.; Demin, I.; Sinitsyn, A.
Monitoring of reactions catalyzed by lytic polysaccharide monooxygenases using highly-sensitive fluorimetric assay of the oxygen consumption rate
Carbohydr. Res.
452
156-161
2017
Thermothelomyces thermophilus (A0A0H4K9X4), Thermothelomyces thermophilus, Thermothielavioides terrestris (D0VWZ9), Thermothielavioides terrestris, Trichoderma reesei (O14405), Trichoderma reesei
brenda
Haske-Cornelius, O.; Pellis, A.; Tegl, G.; Wurz, S.; Saake, B.; Ludwig, R.; Sebastian, A.; Nyanhongo, G.; Guebitz, G.
Enzymatic systems for cellulose acetate degradation
Catalysts
7
187
2017
Neurospora crassa
-
brenda
Sanhueza, C.; Carvajal, G.; Soto-Aguilar, J.; Lienqueo, M.; Salazar, O.
The effect of a lytic polysaccharide monooxygenase and a xylanase from Gloeophyllum trabeum on the enzymatic hydrolysis of lignocellulosic residues using a commercial cellulase
Enzyme Microb. Technol.
113
75-82
2018
Gloeophyllum trabeum, Gloeophyllum trabeum 925-B
brenda
Pierce, B.; Agger, J.; Wichmann, J.; Meyer, A.
Oxidative cleavage and hydrolytic boosting of cellulose in soybean spent flakes by Trichoderma reesei Cel61A lytic polysaccharide monooxygenase
Enzyme Microb. Technol.
98
58-66
2017
Trichoderma reesei (O14405), Trichoderma reesei
brenda
Nekiunaite, L.; Petrovic, D.M.; Westereng, B.; Vaaje-Kolstad, G.; Hachem, M.A.; Varnai, A.; Eijsink, V.G.
FgLPMO9A from Fusarium graminearum cleaves xyloglucan independently of the backbone substitution pattern
FEBS Lett.
590
3346-3356
2016
Fusarium graminearum (I1REU9), Fusarium graminearum ATCC MYA-4620 (I1REU9)
brenda
Hansson, H.; Karkehabadi, S.; Mikkelsen, N.; Douglas, N.; Kim, S.; Lam, A.; Kaper, T.; Kelemen, B.; Meier, K.; Jones, S.; Solomon, E.; Sandgren, M.
High-resolution structure of a lytic polysaccharide monooxygenase from Hypocrea jecorina reveals a predicted linker as an integral part of the catalytic domain
J. Biol. Chem.
292
19099-19109
2017
Trichoderma reesei (G0R6T8), Trichoderma reesei, Trichoderma reesei QM6a (G0R6T8)
brenda
Forsberg, Z.; Bissaro, B.; Gullesen, J.; Dalhus, B.; Vaaje-Kolstad, G.; Eijsink, V.G.H.
Structural determinants of bacterial lytic polysaccharide monooxygenase functionality
J. Biol. Chem.
293
1397-1412
2018
Micromonospora aurantiaca (D9SZQ3), Streptomyces coelicolor (Q9RJC1), Streptomyces coelicolor ATCC BAA-471 (Q9RJC1), Micromonospora aurantiaca DSM 43813 (D9SZQ3)
brenda
Kracher, D.; Andlar, M.; Furtmueller, P.; Ludwig, R.
Active-site copper reduction promotes substrate binding of fungal lytic polysaccharide monooxygenase and reduces stability
J. Biol. Chem.
293
1676-1687
2018
Neurospora crassa
brenda
Hedegard, E.; Ryde, U.
Targeting the reactive intermediate in polysaccharide monooxygenases
J. Biol. Inorg. Chem.
22
1029-1037
2017
Panus similis (A0A0S2GKZ1)
brenda
Couturier, M.; Ladeveze, S.; Sulzenbacher, G.; Ciano, L.; Fanuel, M.; Moreau, C.; Villares, A.; Cathala, B.; Chaspoul, F.; Frandsen, K.; Labourel, A.; Herpoel-Gimbert, I.; Grisel, S.; Haon, M.; Lenfant, N.; Rogniaux, H.; Ropartz, D.; Davies, G.; Rosso,
Lytic xylan oxidases from wood-decay fungi unlock biomass degradation
Nat. Chem. Biol.
14
306-310
2018
Trametes coccinea (A0A2I6QAZ5), Trametes coccinea (A0A2I6QB00)
brenda
Simmons, T.J.; Frandsen, K.E.H.; Ciano, L.; Tryfona, T.; Lenfant, N.; Poulsen, J.C.; Wilson, L.F.L.; Tandrup, T.; Tovborg, M.; Schnorr, K.; Johansen, K.S.; Henrissat, B.; Walton, P.H.; Lo Leggio, L.; Dupree, P.
Structural and electronic determinants of lytic polysaccharide monooxygenase reactivity on polysaccharide substrates
Nat. Commun.
8
1064
2017
Panus similis (A0A0S2GKZ1), Panus similis, Achaetomiella virescens (A0A223GEC9)
brenda
Eibinger, M.; Sattelkow, J.; Ganner, T.; Plank, H.; Nidetzky, B.
Single-molecule study of oxidative enzymatic deconstruction of cellulose
Nat. Commun.
8
894
2017
Neurospora crassa
brenda
Liu, B.; Olson, A.; Wu, M.; Broberg, A.; Sandgren, M.
Biochemical studies of two lytic polysaccharide monooxygenasesfrom the white-rot fungus Heterobasidion irregulare and their roles in lignocellulose degradation
PLoS ONE
12
e0189479
2017
Heterobasidion irregulare
brenda
Tanghe, M.; Danneels, B.; Last, M.; Beerens, K.; Stals, I.; Desmet, T.
Disulfide bridges as essential elements for the thermostability of lytic polysaccharide monooxygenase LPMO10C from Streptomyces coelicolor
Protein Eng. Des. Sel.
30
401-408
2017
Streptomyces coelicolor (Q9RJY2), Streptomyces coelicolor, Streptomyces coelicolor ATCC BAA-471 (Q9RJY2)
brenda
Hu, J.; Tian, D.; Renneckar, S.; Saddler, J.
Enzyme mediated nanofibrillation of cellulose by the synergistic actions of an endoglucanase, lytic polysaccharide monooxygenase (LPMO) and xylanase
Sci. Rep.
8
3195
2018
Thermoascus aurantiacus
brenda