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Information on EC 1.14.99.B10 - lytic xyloglucan monooxygenase
for references in articles please use BRENDA:EC1.14.99.B10
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preliminary BRENDA-supplied EC number
EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.99 Miscellaneous
1.14.99.B10 lytic xyloglucan monooxygenase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
showoxidative cleavage of xyloglucan, cleaving at any position along the beta-glucan backbone, oxidizing at C1 or C4 of D-glucose
Synonyms
gh61-3, ncu02916, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AA9A
EglD
endoglucanase II
gh61-3
GH613
LPMO9A
LPMO9C
LPMO9D
LPMO9E
LPMO9f
LPMO9G
Lpmo9H
LPMOJ
MYCTH_79765
NCU02916
PODANS_4_1020
THITE_2112626
THITE_2122979
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
oxidative cleavage of xyloglucan, cleaving at any position along the beta-glucan backbone, oxidizing at C1 or C4 of D-glucose
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
xyloglucan, hydrogen-donor:oxygen oxidoreductase
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
barely beta-glucan + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: dominance of products increasing by three sugars in size, i.e., DP4, DP7, DP10, DP13, and so forth
Products: dominance of products increasing by three sugars in size, i.e., DP4, DP7, DP10, DP13, and so forth
?
barley mixed-linkage beta-glucan + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: most abundant products show a degree of polymerization of 2-4
Products: most abundant products show a degree of polymerization of 2-4
?
beta-glucan + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
carboxymethyl cellulose + dithiothreitol + O2
carboxymethyl cellooligosaccharides + dithiothreitol disulfide + H2O
cello-oligosaccharides + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: with a degree of polymerization of 5 and 7
Products: -
Products: -
?
cellohexaose + hydroquinone + O2
oxidized cellobiose + oxidized cellotriose + benzoquinone + H2O
Substrates: -
Products: cellohexaose yields both DP2 and DP3 oxidized species
Products: cellohexaose yields both DP2 and DP3 oxidized species
?
cellopentaose + hydroquinone + O2
oxidized cellobiose + oxidized cellotriose + benzoquinone + H2O
cellulose + dithiothreitol + O2
oligosaccharides + dithiothreitol disulfide + H2O
A0A1C9ZMC5, A0A1C9ZP88, A0A1C9ZMC3, A0A1C9ZUN9
Substrates: -
Products: -
Products: -
?
glucomannan + dithiothreitol + O2
cellooligosaccharides + dithiothreitol disulfide + H2O
A0A1C9ZMC5, A0A1C9ZP88, A0A1C9ZMC3, A0A1C9ZUN9
Substrates: -
Products: minor activity on glucomannan
Products: minor activity on glucomannan
?
glucomannan + xylan + ascorbic acid + O2
? + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
low molecular lignin + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
mixed-linkage glucan + ascorbate + O2
? + dehydroascorbate + H2O
-
Substrates: -
Products: -
Products: -
?
phosphoric acid swollen cellulose + ascorbate + O2
cellooligosaccharides + dehydroascorbate + H2O
phosphoric acid swollen cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
Substrates: -
Products: -
Products: -
?
phosphoric acid-swollen cellulose + ascorbate + O2
C1-oxidized xylooligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
reduced xyloglucan oligosaccharide + ascorbic acid + O2
xyloglucan oligosaccharides + dehydroascorbic acid + H2O
Substrates: pure xyloglucan oligosaccharide with DP14
Products: -
Products: -
?
tamarind xyloglucan + ascorbate + O2
C4-oxidized xyloooligosaccharides + dehydroascorbate + H2O
tamarind xyloglucan + ascorbate + O2
C4-oxidized xyloooligosaccharides + dehydroascorbic acid + H2O
tamarind xyloglucan + ascorbic acid + O2
? + dehydroascorbic acid + H2O
Substrates: -
Products: -
Products: -
?
tamarind xyloglucan + ascorbic acid + O2
C1/C4-oxidized xylooligosaccharides + dehydroascorbic acid + H2O
Substrates: -
Products: -
Products: -
?
tamarind xyloglucan + ascorbic acid + O2
C4-oxidized xylooligosaccharides + dehydroascorbic acid + H2O
tamarind xyloglucan + reduced acceptor + O2
C1-oxidized xylooligosaccharides + acceptor + H2O
Substrates: presence of phosphoric acid swollen cellulose is needed to make the LPMOs bind productively to the substrate
Products: -
Products: -
?
tamarind xyloglucan + reduced acceptor + O2
C1/C4-oxidized xylooligosaccharides + acceptor + H2O
Substrates: presence of phosphoric acid swollen cellulose is needed to make the LPMOs bind productively to the substrate
Products: -
Products: -
?
XXXGXXXG + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: branched substrate, G represents an unbranched beta-(1->4)-linked glucosyl residue and X represents beta-(1->4)-linked Glc bearing an alpha-(1->6)-linked xylosyl branch
Products: cleavage generates a gem-diol at the non-reducing end
Products: cleavage generates a gem-diol at the non-reducing end
?
xylan + ascorbate + O2
C1/C4-oxidized xylooligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
xylan + ascorbic acid + O2
? + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
xyloglucan + acceptor + O2
oxidized oligosaccharides + reduced acceptor + H2O
-
Substrates: -
Products: -
Products: -
?
xyloglucan + ascorbate + O2
C1/C4-oxidized oligosaccharides + dehydroascorbate + H2O
-
Substrates: -
Products: -
Products: -
?
xyloglucan + ascorbate + O2
C4-oxidized xylooligosaccharides + C4/C6-oxidized xylooligosaccharides + dehydroascorbate + H2O
-
Substrates: -
Products: -
Products: -
?
xyloglucan + dithiothreitol + O2
xyloglucan oligosaccharides + dithiothreitol disulfide + H2O
A0A1C9ZMC5, A0A1C9ZP88, A0A1C9ZMC3, A0A1C9ZUN9
Substrates: enzyme acts preferentially on free xyloglucan with release of a broad range of xyloglucan oligosaccharides
Products: -
Products: -
?
xyloglucan + reduced acceptor + O2
C1-oxidized xylooligosaccharides + acceptor + H2O
Substrates: poor substrate
Products: -
Products: -
?
xyloglucan 14-mer + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: LPMO9C cuts at the nonreducing end of the intermediate G-unit of a reduced 14-mer derived from tamarind xyloglucan mainly containing XXXGXXXGOH and produces GoxXXXGOH
Products: LPMO9C cuts at the nonreducing end of the intermediate G-unit of a reduced 14-mer derived from tamarind xyloglucan mainly containing XXXGXXXGOH and produces GoxXXXGOH
?
xylogluco-oligosaccharides + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
xylooligosaccharide + pyrogallol + O2
? + H2O
Substrates: -
Products: -
Products: -
?
avicel + ascorbate + O2
oligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: products display a degree of polymerization of DP2 and DP3
Products: products display a degree of polymerization of DP2 and DP3
?
avicel + ascorbate + O2
oligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: products display a degree of polymerization of DP2 and DP3
Products: products display a degree of polymerization of DP2 and DP3
?
carboxymethyl cellulose + dithiothreitol + O2
carboxymethyl cellooligosaccharides + dithiothreitol disulfide + H2O
A0A1C9ZMC5, A0A1C9ZP88, A0A1C9ZMC3, A0A1C9ZUN9
Substrates: reaction is slower with electron donor dithiothreitol than with ascorbate. Reaction is 5- to 10fold slower with carboxymethyl cellulose than with xyloglucan
Products: -
Products: -
?
carboxymethyl cellulose + dithiothreitol + O2
carboxymethyl cellooligosaccharides + dithiothreitol disulfide + H2O
A0A1C9ZMC5, A0A1C9ZP88, A0A1C9ZMC3, A0A1C9ZUN9
Substrates: -
Products: -
Products: -
?
carboxymethyl cellulose + dithiothreitol + O2
carboxymethyl cellooligosaccharides + dithiothreitol disulfide + H2O
A0A1C9ZMC5, A0A1C9ZP88, A0A1C9ZMC3, A0A1C9ZUN9
Substrates: reaction is slower with electron donor dithiothreitol than with ascorbate. Reaction is 5- to 10fold slower with carboxymethyl cellulose than with xyloglucan
Products: -
Products: -
?
cellopentaose + hydroquinone + O2
oxidized cellobiose + oxidized cellotriose + benzoquinone + H2O
Substrates: -
Products: -
Products: -
?
cellopentaose + hydroquinone + O2
oxidized cellobiose + oxidized cellotriose + benzoquinone + H2O
Substrates: -
Products: -
Products: -
?
cellulose + ascorbate + O2
cellooligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: cleavage generates singly and doubly oxidized products at the C1 and/or C4 positions
Products: cleavage generates singly and doubly oxidized products at the C1 and/or C4 positions
?
cellulose + ascorbate + O2
cellooligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: cleavage generates singly and doubly oxidized products at the C1 and/or C4 positions
Products: cleavage generates singly and doubly oxidized products at the C1 and/or C4 positions
?
cellulose hexasaccharide + acceptor + O2
? + reduced acceptor + H2O
Substrates: -
Products: -
Products: -
?
cellulose hexasaccharide + acceptor + O2
? + reduced acceptor + H2O
Substrates: -
Products: -
Products: -
?
glucomannan + ascorbate + O2
? + dehydroascorbate + H2O
-
Substrates: -
Products: -
Products: -
?
glucomannan + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: release of clusters of products up to at least a degree of polymersation DP15, each cluster containing the keto-, gemdiol and native form of hexose oligosaccharides and acetylated species
Products: release of clusters of products up to at least a degree of polymersation DP15, each cluster containing the keto-, gemdiol and native form of hexose oligosaccharides and acetylated species
?
glucomannan + ascorbate + O2
cellooligosaccharides + dehydroascorbate + H2O
A0A1C9ZMC5, A0A1C9ZP88, A0A1C9ZMC3, A0A1C9ZUN9
Substrates: -
Products: -
Products: -
?
glucomannan + ascorbate + O2
cellooligosaccharides + dehydroascorbate + H2O
A0A1C9ZMC5, A0A1C9ZP88, A0A1C9ZMC3, A0A1C9ZUN9
Substrates: -
Products: -
Products: -
?
konjac glucomannan + ascorbate + O2
cellooligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: products are aldonic acids and gem-diols
Products: products are aldonic acids and gem-diols
?
konjac glucomannan + ascorbate + O2
cellooligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: products are aldonic acids and gem-diols
Products: products are aldonic acids and gem-diols
?
lichenan + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
lichenan + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: most abundant products show a degree of polymerization of 2-4
Products: most abundant products show a degree of polymerization of 2-4
?
lichenan + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: most abundant products show a degree of polymerization of 2-4
Products: most abundant products show a degree of polymerization of 2-4
?
phosphoric acid swollen cellulose + ascorbate + O2
cellooligosaccharides + dehydroascorbate + H2O
A0A1C9ZMC5, A0A1C9ZP88, A0A1C9ZMC3, A0A1C9ZUN9
Substrates: -
Products: -
Products: -
?
phosphoric acid swollen cellulose + ascorbate + O2
cellooligosaccharides + dehydroascorbate + H2O
A0A1C9ZMC5, A0A1C9ZP88, A0A1C9ZMC3, A0A1C9ZUN9
Substrates: -
Products: -
Products: -
?
phosphoric acid swollen cellulose + catechin + O2
cello-oligosaccharides + ? + H2O
Substrates: -
Products: products display a degree of polymerization of DP2 and DP3
Products: products display a degree of polymerization of DP2 and DP3
?
phosphoric acid swollen cellulose + catechin + O2
cello-oligosaccharides + ? + H2O
Substrates: -
Products: products display a degree of polymerization of DP2 and DP3
Products: products display a degree of polymerization of DP2 and DP3
?
polymeric xyloglucan + acceptor + O2
? + reduced acceptor + H2O
Substrates: -
Products: -
Products: -
?
polymeric xyloglucan + acceptor + O2
? + reduced acceptor + H2O
Substrates: -
Products: -
Products: -
?
steam-exploded spruce + ascorbate + O2
oligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: products display a degree of polymerization of DP2 and DP3
Products: products display a degree of polymerization of DP2 and DP3
?
steam-exploded spruce + ascorbate + O2
oligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: products display a degree of polymerization of DP2 and DP3
Products: products display a degree of polymerization of DP2 and DP3
?
tamarind xyloglucan + 2 cysteine + O2
? + cystine + H2O
-
Substrates: -
Products: -
Products: -
?
tamarind xyloglucan + 2 cysteine + O2
? + cystine + H2O
Substrates: -
Products: -
Products: -
?
tamarind xyloglucan + 2 cysteine + O2
? + cystine + H2O
Substrates: -
Products: -
Products: -
?
tamarind xyloglucan + 2 cysteine + O2
? + cystine + H2O
-
Substrates: -
Products: -
Products: -
?
tamarind xyloglucan + 2 cysteine + O2
? + cystine + H2O
A0A5S8WF95
Substrates: -
Products: -
Products: -
?
tamarind xyloglucan + 2 cysteine + O2
? + cystine + H2O
-
Substrates: -
Products: -
Products: -
?
tamarind xyloglucan + 2 cysteine + O2
? + cystine + H2O
-
Substrates: -
Products: -
Products: -
?
tamarind xyloglucan + 2 cysteine + O2
? + cystine + H2O
-
Substrates: -
Products: -
Products: -
?
tamarind xyloglucan + ascorbate + O2
C4-oxidized xyloooligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
tamarind xyloglucan + ascorbate + O2
C4-oxidized xyloooligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
tamarind xyloglucan + ascorbate + O2
C4-oxidized xyloooligosaccharides + dehydroascorbic acid + H2O
Substrates: -
Products: -
Products: -
?
tamarind xyloglucan + ascorbate + O2
C4-oxidized xyloooligosaccharides + dehydroascorbic acid + H2O
Substrates: -
Products: -
Products: -
?
tamarind xyloglucan + ascorbate + O2
xylooligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: products are mostly oligosaccharides having degrees of polymerization of 6 and 7
Products: products are mostly oligosaccharides having degrees of polymerization of 6 and 7
?
tamarind xyloglucan + ascorbate + O2
xylooligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: products are mostly oligosaccharides having degrees of polymerization of 6 and 7
Products: products are mostly oligosaccharides having degrees of polymerization of 6 and 7
?
tamarind xyloglucan + ascorbic acid + O2
C4-oxidized xylooligosaccharides + dehydroascorbic acid + H2O
Substrates: -
Products: -
Products: -
?
tamarind xyloglucan + ascorbic acid + O2
C4-oxidized xylooligosaccharides + dehydroascorbic acid + H2O
Thermothelomyces thermophilus DSM 1799
Substrates: -
Products: -
Products: -
?
thio-linked cello-oligosaccharides + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: with a degree of polymerization of 25
Products: -
Products: -
?
thio-linked cello-oligosaccharides + ascorbate + O2
? + dehydroascorbate + H2O
-
Substrates: with a degree of polymerization of 25
Products: -
Products: -
?
thio-linked xylopentaose + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
thio-linked xylopentaose + ascorbate + O2
? + dehydroascorbate + H2O
-
Substrates: -
Products: -
Products: -
?
xyloglucan + ascorbate + O2
? + dehydroascorbate + H2O
-
Substrates: -
Products: -
Products: -
?
xyloglucan + ascorbate + O2
? + dehydroascorbate + H2O
A0A1C9ZMC5, A0A1C9ZP88, A0A1C9ZMC3, A0A1C9ZUN9
Substrates: -
Products: releases a broad range of xyloglucan oligosaccharides, cleaving occurs at any position along the beta-glucan backbone of xyloglucan, regardless of substitutions. Dominating products contain a four-glucan backbone (XXXG fragments with various degrees of galactosylation), plus C-1-oxidized and C-4-oxidized cellooligosaccharides
Products: releases a broad range of xyloglucan oligosaccharides, cleaving occurs at any position along the beta-glucan backbone of xyloglucan, regardless of substitutions. Dominating products contain a four-glucan backbone (XXXG fragments with various degrees of galactosylation), plus C-1-oxidized and C-4-oxidized cellooligosaccharides
?
xyloglucan + ascorbate + O2
? + dehydroascorbate + H2O
A0A1C9ZMC5, A0A1C9ZP88, A0A1C9ZMC3, A0A1C9ZUN9
Substrates: -
Products: releases a broad range of xyloglucan oligosaccharides, cleaving occurs at any position along the beta-glucan backbone of xyloglucan, regardless of substitutions. Dominating products contain a four-glucan backbone (XXXG fragments with various degrees of galactosylation), plus C-1-oxidized and C-4-oxidized cellooligosaccharides
Products: releases a broad range of xyloglucan oligosaccharides, cleaving occurs at any position along the beta-glucan backbone of xyloglucan, regardless of substitutions. Dominating products contain a four-glucan backbone (XXXG fragments with various degrees of galactosylation), plus C-1-oxidized and C-4-oxidized cellooligosaccharides
?
xyloglucan + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: two major oxidized products corresponding to the keto-form of single oxidized species, the most probable product configurations being GoxXXL and GoxXLL
Products: two major oxidized products corresponding to the keto-form of single oxidized species, the most probable product configurations being GoxXXL and GoxXLL
?
xyloglucan + ascorbate + O2
C1/C4-oxidized xylooligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
xyloglucan + ascorbate + O2
C1/C4-oxidized xylooligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
xyloglucan 14-mer + acceptor + O2
? + reduced acceptor + H2O
Substrates: -
Products: -
Products: -
?
xyloglucan 14-mer + acceptor + O2
? + reduced acceptor + H2O
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: xylan, starch, laminarin, chitin. cleavage of cleavage of hemicelluloses and phosphoric acid swollen cellulose C uses both C1- and C4-oxidizing mechanisms
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme also catalyzes degradation of avicel, reaction of EC 1.14.99.54
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme produces C4-oxidized products from cellulose with no evidence of C1 oxidation, cf. EC 1.14.99.56
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme produces C4-oxidized products from cellulose with no evidence of C1 oxidation
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoforms AA9A and AA9B react on cellulose and on xyloglucan
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme produces C4-oxidized products from cellulose with no evidence of C1 oxidation, cgf. EC 1.14.99.56
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme catalyzes mixed C1/C4 oxidative cleavage of cellulose, reactions of EC 1.14.99.54 and EC1.14.99.56, and xyloglucan, 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: inactive on shorter cellooligosaccharides, such as cellopentaose and cellohexaose, and on arabinoxylan, ivory nut mannan, wheat arabinoxylan, oat spelt xylan, beech wood xylan, and birchwood xylan or mixed linked beta-glucan. Presence of an electron donor is required
Products: -
Products: -
?
additional information
?
-
A0A1C9ZMC5
Substrates: inactive on shorter cellooligosaccharides, such as cellopentaose and cellohexaose, and on arabinoxylan, ivory nut mannan, wheat arabinoxylan, oat spelt xylan, beech wood xylan, and birchwood xylan or mixed linked beta-glucan. Presence of an electron donor is required
Products: -
Products: -
?
additional information
?
-
Substrates: inactive on shorter cellooligosaccharides, such as cellopentaose and cellohexaose, and on arabinoxylan, ivory nut mannan, wheat arabinoxylan, oat spelt xylan, beech wood xylan, and birchwood xylan or mixed linked beta-glucan. Presence of an electron donor is required
Products: -
Products: -
?
additional information
?
-
Substrates: inactive on shorter cellooligosaccharides, such as cellopentaose and cellohexaose, and on arabinoxylan, ivory nut mannan, wheat arabinoxylan, oat spelt xylan, beech wood xylan, and birchwood xylan or mixed linked beta-glucan. Presence of an electron donor is required
Products: -
Products: -
?
additional information
?
-
Substrates: inactive on shorter cellooligosaccharides, such as cellopentaose and cellohexaose, and on arabinoxylan, ivory nut mannan, wheat arabinoxylan, oat spelt xylan, beech wood xylan, and birchwood xylan or mixed linked beta-glucan. Presence of an electron donor is required
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoform LpmoA-2 has broad specificity, cleaving at any position along the beta-glucan backbone of xyloglucan, regardless of substitutions. Inactive on shorter cello-oligosaccharides, such as cellopentaose and cellohexaose, and on arabinoxylan
Products: -
Products: -
?
additional information
?
-
A0A1C9ZMC5
Substrates: isoform LpmoA-2 has broad specificity, cleaving at any position along the beta-glucan backbone of xyloglucan, regardless of substitutions. Inactive on shorter cello-oligosaccharides, such as cellopentaose and cellohexaose, and on arabinoxylan
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additional information
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Substrates: isoform LpmoA-2 has broad specificity, cleaving at any position along the beta-glucan backbone of xyloglucan, regardless of substitutions. Inactive on shorter cello-oligosaccharides, such as cellopentaose and cellohexaose, and on arabinoxylan
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additional information
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Substrates: isoform LpmoA-2 has broad specificity, cleaving at any position along the beta-glucan backbone of xyloglucan, regardless of substitutions. Inactive on shorter cello-oligosaccharides, such as cellopentaose and cellohexaose, and on arabinoxylan
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additional information
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Substrates: isoform LpmoA-2 has broad specificity, cleaving at any position along the beta-glucan backbone of xyloglucan, regardless of substitutions. Inactive on shorter cello-oligosaccharides, such as cellopentaose and cellohexaose, and on arabinoxylan
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additional information
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Substrates: gradual addition of H2O2 allows LPMO activity at very low, substoichiometric reductant concentrations. Enzyme accepts ascorbate and gallate as reductant, but not 2,3-dihydroxybenzoate under standard aerobic conditions. 2,3-dihydroxybenzoate is accepted in the presence of externally added H2O2 and at alkaline pH it is able to drive the LPMO reaction without externally added H2O2. No substrates: phosphoric acid-swollen cellulose, soluble cello-oligosaccharides (Glc5 and Glc6), konjac glucomannan, lichenan from Icelandic moss, birchwood xylan, galactomannan, wheat arabinoxylan, barley beta-glucan, ivory nut mannan
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additional information
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A0A1C9ZMC5
Substrates: inactive on shorter cellooligosaccharides, such as cellopentaose and cellohexaose, and on arabinoxylan, ivory nut mannan, wheat arabinoxylan, oat spelt xylan, beech wood xylan, and birchwood xylan or mixed linked beta-glucan. Presence of an electron donor is required
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additional information
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Substrates: inactive on shorter cellooligosaccharides, such as cellopentaose and cellohexaose, and on arabinoxylan, ivory nut mannan, wheat arabinoxylan, oat spelt xylan, beech wood xylan, and birchwood xylan or mixed linked beta-glucan. Presence of an electron donor is required
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additional information
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Substrates: inactive on shorter cellooligosaccharides, such as cellopentaose and cellohexaose, and on arabinoxylan, ivory nut mannan, wheat arabinoxylan, oat spelt xylan, beech wood xylan, and birchwood xylan or mixed linked beta-glucan. Presence of an electron donor is required
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additional information
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Substrates: inactive on shorter cellooligosaccharides, such as cellopentaose and cellohexaose, and on arabinoxylan, ivory nut mannan, wheat arabinoxylan, oat spelt xylan, beech wood xylan, and birchwood xylan or mixed linked beta-glucan. Presence of an electron donor is required
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additional information
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Substrates: preferentially cleaves residual xylan in phosphoric acid-swollen cellulose, primarily producing C1-oxidized cellooligosaccharides. When exposed to cellulose-xylan blends, AA9H shows a preference for xylan and for releasing (oxidized) xylooligosaccharides. No activity with tamarind xyloglucan alone, but generates products in reaction mixtures containing both cellulose and tamarind xyloglucan
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additional information
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Substrates: preferentially cleaves residual xylan in phosphoric acid-swollen cellulose, primarily producing C1-oxidized cellooligosaccharides. When exposed to cellulose-xylan blends, AA9H shows a preference for xylan and for releasing (oxidized) xylooligosaccharides. No activity with tamarind xyloglucan alone, but generates products in reaction mixtures containing both cellulose and tamarind xyloglucan
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additional information
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Substrates: preferentially cleaves residual xylan in phosphoric acid-swollen cellulose, primarily producing C1-oxidized cellooligosaccharides. When exposed to cellulose-xylan blends, AA9H shows a preference for xylan and for releasing (oxidized) xylooligosaccharides. No activity with tamarind xyloglucan alone, but generates products in reaction mixtures containing both cellulose and tamarind xyloglucan
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additional information
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Substrates: preferentially cleaves residual xylan in phosphoric acid-swollen cellulose, primarily producing C1-oxidized cellooligosaccharides. When exposed to cellulose-xylan blends, AA9H shows a preference for xylan and for releasing (oxidized) xylooligosaccharides. No activity with tamarind xyloglucan alone, but generates products in reaction mixtures containing both cellulose and tamarind xyloglucan
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additional information
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Substrates: enzyme acts both on cellulose and on noncellulose beta-glucans, including cellodextrins and xyloglucan
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additional information
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Substrates: enzyme particularly acts on the glucose backbone of xyloglucan, accepting various substitutions (xylose, galactose) in almost all positions. It requires short stretches of contiguous (1->4)-beta-linked glucose units for activity. No substrates: (1->4)-beta-D-xylan, (1->4)-alpha-D-polygalacturonan, (1->4)-beta-D-mannan, (1->4)-beta-D-galactan, yeast beta-D-glucan, callose, and arabinoxylan
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additional information
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Substrates: substrate binding has a substantial effect on the chemical shifts of residues His1, Ala80, His83 and His155
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additional information
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Substrates: products released contain a C4 gemdiol/keto group at the nonreducing end. Hydroquinone, ascorbic acid, and catechin serve equally well as reductant. No substrates: mannohexaose, xylopentaose, xylohexaose, chitopentaose, and maltodextrin
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additional information
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-
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Substrates: products released contain a C4 gemdiol/keto group at the nonreducing end. Hydroquinone, ascorbic acid, and catechin serve equally well as reductant. No substrates: mannohexaose, xylopentaose, xylohexaose, chitopentaose, and maltodextrin
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additional information
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Substrates: enzyme exclusively oxidizes at C4. Enzyme efficiently uses H2O2 as a cosubstrate, yielding product profiles identical to those obtained in O2-driven reactions with phosphoric acid-swollen cellulose, xyloglucan, or glucomannan
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additional information
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Substrates: enzyme exclusively oxidizes at C4. Enzyme efficiently uses H2O2 as a cosubstrate, yielding product profiles identical to those obtained in O2-driven reactions with phosphoric acid-swollen cellulose, xyloglucan, or glucomannan
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additional information
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Substrates: enzyme exclusively oxidizes at C4. Enzyme efficiently uses H2O2 as a cosubstrate, yielding product profiles identical to those obtained in O2-driven reactions with phosphoric acid-swollen cellulose, xyloglucan, or glucomannan
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additional information
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Substrates: acts on cellooligosaccharides with degree of polymerization above 5, xyloglucan, glucomannan, and x02beta-glucan, exclusively products oxidized at the C4 position are found. Enzyme efficiently uses H2O2 as a cosubstrate, yielding product profiles identical to those obtained in O2-driven reactions with phosphoric acid-swollen cellulose, xyloglucan, or glucomannan
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additional information
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Substrates: acts on cellooligosaccharides with degree of polymerization above 5, xyloglucan, glucomannan, and x02beta-glucan, exclusively products oxidized at the C4 position are found. Enzyme efficiently uses H2O2 as a cosubstrate, yielding product profiles identical to those obtained in O2-driven reactions with phosphoric acid-swollen cellulose, xyloglucan, or glucomannan
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additional information
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Substrates: acts on cellooligosaccharides with degree of polymerization above 5, xyloglucan, glucomannan, and x02beta-glucan, exclusively products oxidized at the C4 position are found. Enzyme efficiently uses H2O2 as a cosubstrate, yielding product profiles identical to those obtained in O2-driven reactions with phosphoric acid-swollen cellulose, xyloglucan, or glucomannan
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additional information
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-
-
Substrates: enzyme acts both on cellulose and on noncellulose beta-glucans, including cellodextrins and xyloglucan
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additional information
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Substrates: substrate binding has a substantial effect on the chemical shifts of residues His1, Ala80, His83 and His155
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additional information
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Substrates: products released contain a C4 gemdiol/keto group at the nonreducing end. Hydroquinone, ascorbic acid, and catechin serve equally well as reductant. No substrates: mannohexaose, xylopentaose, xylohexaose, chitopentaose, and maltodextrin
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additional information
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Substrates: enzyme exclusively oxidizes at C4. Enzyme efficiently uses H2O2 as a cosubstrate, yielding product profiles identical to those obtained in O2-driven reactions with phosphoric acid-swollen cellulose, xyloglucan, or glucomannan
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additional information
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Substrates: enzyme exclusively oxidizes at C4. Enzyme efficiently uses H2O2 as a cosubstrate, yielding product profiles identical to those obtained in O2-driven reactions with phosphoric acid-swollen cellulose, xyloglucan, or glucomannan
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additional information
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Substrates: enzyme exclusively oxidizes at C4. Enzyme efficiently uses H2O2 as a cosubstrate, yielding product profiles identical to those obtained in O2-driven reactions with phosphoric acid-swollen cellulose, xyloglucan, or glucomannan
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additional information
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Substrates: acts on cellooligosaccharides with degree of polymerization above 5, xyloglucan, glucomannan, and x02beta-glucan, exclusively products oxidized at the C4 position are found. Enzyme efficiently uses H2O2 as a cosubstrate, yielding product profiles identical to those obtained in O2-driven reactions with phosphoric acid-swollen cellulose, xyloglucan, or glucomannan
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additional information
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Substrates: acts on cellooligosaccharides with degree of polymerization above 5, xyloglucan, glucomannan, and x02beta-glucan, exclusively products oxidized at the C4 position are found. Enzyme efficiently uses H2O2 as a cosubstrate, yielding product profiles identical to those obtained in O2-driven reactions with phosphoric acid-swollen cellulose, xyloglucan, or glucomannan
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additional information
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Substrates: acts on cellooligosaccharides with degree of polymerization above 5, xyloglucan, glucomannan, and x02beta-glucan, exclusively products oxidized at the C4 position are found. Enzyme efficiently uses H2O2 as a cosubstrate, yielding product profiles identical to those obtained in O2-driven reactions with phosphoric acid-swollen cellulose, xyloglucan, or glucomannan
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additional information
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Substrates: enzyme cleaves cellulose, xyloglucan, 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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A0A5S8WF95
Substrates: enzyme produces C4-oxidized products from cellulose with no evidence of C1 oxidation, cf. EC 1.14.99.56
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additional information
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Substrates: enzyme exhibits a mixed C1/C4 oxidative cleavage activity on cellulose and xyloglucan, but not on xylan
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additional information
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-
-
Substrates: enzyme produces C4-oxidized products from cellulose with no evidence of C1 oxidation, cf. EC 1.14.99.56
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additional information
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-
-
Substrates: enzyme produces C4-oxidized products from cellulose with no evidence of C1 oxidation, cf. EC 1.14.99.56
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additional information
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Substrates: LPMO9H is able to target polysaccharides differing from cellulose by their linkage types, glycosidic composition or the presence of sidechains. Isoform LPMO9H catalyzes C4 oxidative cleavage of mixed-linkage glucans, and mixed C1/C4 oxidative cleavage of glucomannan and xyloglucan. Gem-diols and ketones are produced at the non-reducing end, while aldonic acids are produced at the reducing extremity of the products
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additional information
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Substrates: LPMO9H is able to target polysaccharides differing from cellulose by their linkage types, glycosidic composition or the presence of sidechains. Isoform LPMO9H catalyzes C4 oxidative cleavage of mixed-linkage glucans, and mixed C1/C4 oxidative cleavage of glucomannan and xyloglucan. Gem-diols and ketones are produced at the non-reducing end, while aldonic acids are produced at the reducing extremity of the products
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additional information
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-
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Substrates: enzyme produces C4-oxidized products from cellulose with no evidence of C1 oxidation, cf. EC 1.14.99.56
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additional information
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Substrates: enzyme shows activity toward PASC, tamarind xyloglucan and steam-exploded birch in the presence of ascorbic acid, while it is inactive toward cellopentaose, ivory nut mannan, konjac glucomannan, and xylan from birch wood. In the presence of ascorbic acid, LPMO9A releases a mixture of C1- and C4-oxidized oligosaccharides
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additional information
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Substrates: in the absence of substrate with ascorbate as reductant, enzyme shows a H2O2 production rate of about 1.00 per min
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additional information
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Substrates: enzyme performs C4-oxidation and is active against cellulose, soluble cello-oligosaccharides, cf. EC 1.14.99.56, and xyloglucan. No substrates: konjac glucomannan, barley beta-glucan and sugar beet arabinan
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-
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Substrates: additionally catalyzes the reaction with cellulose, EC 1.14.99.54 and EC 1.14.99.56
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additional information
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Thermothelomyces thermophilus DSM 1799
Substrates: enzyme performs C4-oxidation and is active against cellulose, soluble cello-oligosaccharides, cf. EC 1.14.99.56, and xyloglucan. No substrates: konjac glucomannan, barley beta-glucan and sugar beet arabinan
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additional information
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Substrates: enzyme produces hydrogen peroxide in the absence of polysaccharide substrate and displays peroxidase-like activity. Enzyme is active on xyloglucan. No substrates: wheat arabinoxylan, konjac glucomannan, acetylated spruce galactoglucomannan, or cellopentaose
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additional information
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Substrates: enzyme produces hydrogen peroxide in the absence of polysaccharide substrate and displays peroxidase-like activity. Enzyme is active on xyloglucan. No substrates: wheat arabinoxylan, konjac glucomannan, acetylated spruce galactoglucomannan, or cellopentaose
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additional information
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Substrates: enzyme produces hydrogen peroxide in the absence of polysaccharide substrate and displays peroxidase-like activity. Enzyme is active on xyloglucan. No substrates: wheat arabinoxylan, konjac glucomannan, acetylated spruce galactoglucomannan, or cellopentaose
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additional information
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Substrates: enzyme produces hydrogen peroxide in the absence of polysaccharide substrate and displays peroxidase-like activity. Enzyme is active on xyloglucan. No substrates: wheat arabinoxylan, konjac glucomannan, acetylated spruce galactoglucomannan, or cellopentaose
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additional information
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Substrates: enzyme produces hydrogen peroxide in the absence of polysaccharide substrate and displays peroxidase-like activity. Enzyme is active on xyloglucan. No substrates: wheat arabinoxylan, konjac glucomannan, acetylated spruce galactoglucomannan, or cellopentaose
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additional information
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Substrates: enzyme produces hydrogen peroxide in the absence of polysaccharide substrate and displays peroxidase-like activity. Enzyme is active on xyloglucan. No substrates: wheat arabinoxylan, konjac glucomannan, acetylated spruce galactoglucomannan, or cellopentaose
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
in the absence of electron donor, such as ascorbic acid, no reaction is detected
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
Cu2+
copper
-
reduction of the mononuclear active-site copper by ascorbic acid increases the affinity and the maximum binding capacity of LPMO for cellulose, reaction of EC 1.14.99.54. The reduced redox state of the active-site copper and not the subsequent formation of the activated oxygen species increase the affinity toward cellulose
Cu2+
the Cu+ center environment is altered upon substrate binding. The oxidative regioselectivity of LPMO9 enzymes (C1, C4, or both) correlates with distinct structural features of the copper coordination sphere. In strictly C1-oxidizing LPMO9s, access to the solvent-facing axial coordination position is restricted by a conserved tyrosine residue, whereas access to this same position seems unrestricted in C4-oxidizing LPMO9s
Cu2+
the copper ion alone hardly contributes to affinity, but substrate binding is enhanced for metal-loaded enzymes that are supplied with cyanide
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
H2O2
low concentrations of H2O2 boost LPMO activity, whereas excess H2O2 leads to LPMO inactivation
additional information
-
hemicellulose coating has an inhibitory effect on cellulolytic LPMO activity
-
additional information
A0A1C9ZMC5
hemicellulose coating has an inhibitory effect on cellulolytic LPMO activity
-
additional information
hemicellulose coating has an inhibitory effect on cellulolytic LPMO activity
-
additional information
hemicellulose coating has an inhibitory effect on cellulolytic LPMO activity
-
additional information
hemicellulose coating has an inhibitory effect on cellulolytic LPMO activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cyanide
substrate binding is enhanced for metal-loaded enzymes that are supplied with cyanide
H2O2
low concentrations of H2O2 boost LPMO activity, whereas excess H2O2 leads to LPMO inactivation
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9 - 10
-
enzyme activity starts decreasing after approximately 700 s, while the enzymatic activity continues until the end of the experiment at pHs 6.0 and 7.0
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
splice variant LPMO9A-2, which contains a C-terminal domain comprising approximately 55 residues without a predicted function
A0A1C9ZMC5
UniProt
brenda
splice variant LPMO9A-2, which contains a C-terminal domain comprising approximately 55 residues without a predicted function
A0A1C9ZMC5
UniProt
brenda
cf. EC 3.2.1.4, EC 3.2.1.54, EC 1.14.99.56
UniProt
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
enzyme acts in synergy with cellobiose dehydrogenase. The cytochrome domain of cellobiose dehydrogenase interacts with the copper site of the LPMO and substrate binding precludes interaction with cellobiose dehydrogenase
physiological function
-
enzyme acts in synergy with cellobiose dehydrogenase. The cytochrome domain of cellobiose dehydrogenase interacts with the copper site of the LPMO and substrate binding precludes interaction with cellobiose dehydrogenase
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LP9H_MALCI
230
0
24333
Swiss-Prot
other Location (Reliability: 2)
LP9H_PODAN
Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
370
0
38952
Swiss-Prot
-
G2Q7A5_THET4
Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799)
246
0
26044
TrEMBL
other Location (Reliability: 1)
LP9G_THETT
Thermothielavioides terrestris (strain ATCC 38088 / NRRL 8126)
304
0
31783
Swiss-Prot
-
LP9A_THETT
Thermothielavioides terrestris (strain ATCC 38088 / NRRL 8126)
233
0
24424
Swiss-Prot
-
LP9E_THETT
Thermothielavioides terrestris (strain ATCC 38088 / NRRL 8126)
226
0
24213
Swiss-Prot
-
LP9A_GIBZE
Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1)
335
0
34294
Swiss-Prot
-
LPMO_NEUCR
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
238
0
24705
Swiss-Prot
-
LP9A_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
367
0
38033
Swiss-Prot
-
LP9C_ASPFU
Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)
349
0
35735
Swiss-Prot
other Location (Reliability: 2)
LP9A_NEUCR
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
322
0
32802
Swiss-Prot
Secretory Pathway (Reliability: 1)
LP9C_NEUCR
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
359
0
35755
Swiss-Prot
-
LP9B_GLOTA
Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617)
252
0
26624
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 27000, SDS-PAGE, x * 23000, calculated for isoform AA9A, x * 29000, SDS-PAGE, x * 24000, calculated for isoform AA9B, respectively
?
Aspergillus tamarii CBS 117626
-
x * 27000, SDS-PAGE, x * 23000, calculated for isoform AA9A, x * 29000, SDS-PAGE, x * 24000, calculated for isoform AA9B, respectively
-
?
x * 30000, SDS-PAGE, x * 27000 after deglycosylation with Endo Hf
?
x * 25000-30000, SDS-PAGE, x * 24400, calculated from sequnce
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
A0A1C9ZMC5, A0A1C9ZP88, A0A1C9ZMC3, A0A1C9ZUN9
treatment with EndoH leads to a decrease in molecular mass from 60 kDA to 57 kDa
glycoprotein
A0A1C9ZMC5, A0A1C9ZP88, A0A1C9ZMC3, A0A1C9ZUN9
treatment with EndoH leads to a decrease in molecular mass from 60000 Da to 57000 Da
glycoprotein
-
treatment with EndoH leads to a decrease in molecular mass from 60 kDA to 57 kDa
-
glycoprotein
molecular mass decreases by 3000 Da after deglycosylation with Endo Hf. Putative N-glycosylation sites are N34 and N80
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of AA9A bound to cellulosic and non-cellulosic oligosaccharides
-
1H, 13C, and 15N chemical shift assignments of the apo-form of the catalytic doman
crystals grown in presence of Zn2+ and of Cu2+. Structure of the catalytic domain reveals an extended, highly polar substrate-binding surface well suited to interact with a variety of sugar substrates. Binding affinities are in the low micromolar range for polymeric substrates due in part to the presence of a carbohydrate-binding module
docking studies with cellulose hexamer. The surface patch surrounding the copper site appears to be a preferred interaction surface. Residue Tyr204 appears not to be involved in binding of this substrate
structure of copper-bound monooxygnase LPMO9A at 1.6 A resolution. Isoforms LPMO9A and LPMO9C, containing a CBM1 carbohydrate-binding module, bind cellulose more strongly and are less susceptible to inactivation than LPMO9D, which lacks a CBM
structure of AA9A bound to cellulosic and non-cellulosic oligosaccharides
low-resolution SAXS LPMO9H structure in solution. The position of CBM1 lies within the tail of the tadpole appended via long linker peptide to the catalytic domain which can be placed in its head
-
homology model shows typical and complete LPMO structures
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
variants of LPMO9A, with and without the methylation on His1 are identical in terms of substrate preferences, cleavage specificities and the ability to activate molecular oxygen. The ability to cleave xyloglucan is identical for both variants. Methylation has minimal effects on the pKa of His1, the affinity for copper and the redox potential of bound copper. The variants show clear differences in their resistance against oxidative damage, the methylated variant, produced in Aspergillus oryzae, is more resistant to excess H2O2
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60.4
-
melting temperature, presence of 2 mM ascorbate and 2 mg/ml xyloglucan
62
-
melting temperature, presence of 2 mM ascorbate and 2 mg/ml xyloglucan
additional information
-
stabilizing effect of the substrates cellulose and xyloglucan on the apparent transition midpoint temperature of the reduced, catalytically active enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein, purified by step-wise anion exchange chromatography, size exclusion chromatography and cation exchange chromatography
-
recombinant protein, purified from culture medium in two chromatographic steps to ca. 95% purity
recombinant protein, using hydrophobic interaction chromatography followed by size exclusion chromatography
recombinant proteins, starting with anion exchange chromatography followed by size exclusion chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Pichia pastoris
expression of splice variant LPMO9A-2 in Pichia pastoris
A0A1C9ZMC5, A0A1C9ZP88, A0A1C9ZMC3, A0A1C9ZUN9
expression of splice variant LpmoA-2 in Pichia pastoris
A0A1C9ZMC5, A0A1C9ZP88, A0A1C9ZMC3, A0A1C9ZUN9
homologous expression in a low protease/low hemicellulase/low cellulase producing Myceliophthora thermophila strain
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
degradation
enzyme shows a higher boosting effect on the enzymatic saccharification of complex lignocellulosic substrates associated with xyloglucan than on the lignocellulosic substrates without xyloglucan particularly in low commercial cellulase dosage cases
degradation
-
product formation is remarkably increased when LPMO9H is combined with GH7 endoglucanase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
brenda
Kojima, Y.; Vrnai, A.; Ishida, T.; Sunagawa, N.; Petrovic, D.M.; Igarashi, K., Jellison, J.; Goodell, B.; Alfredsen, G.; Westereng, B.; Eijsink, V.G.; Yoshida, M.
A lytic polysaccharide monooxygenase with broad xyloglucan specificity from the brown-rot fungus Gloeophyllum trabeum and its action on cellulose-xyloglucan complexes
Appl. Environ. Microbiol.
82
6557-6572
2016
Gloeophyllum trabeum, Gloeophyllum trabeum (A0A1C9ZMC5), Gloeophyllum trabeum (A0A1C9ZP88), Gloeophyllum trabeum (A0A1C9ZMC3), Gloeophyllum trabeum (A0A1C9ZUN9), Gloeophyllum trabeum NBRC 6430 (A0A1C9ZMC5), Gloeophyllum trabeum NBRC 6430 (A0A1C9ZP88), Gloeophyllum trabeum NBRC 6430 (A0A1C9ZMC3), Gloeophyllum trabeum NBRC 6430 (A0A1C9ZUN9)
brenda
Courtade, G.; Wimmer, R.; Dimarogona, M.; Sandgren, M.; Eijsink, V.; Aachmann, F.
Backbone and side-chain 1H, 13C, and 15N chemical shift assignments for the apo-form of the lytic polysaccharide monooxygenase NcLPMO9C
Biomol. NMR Assign.
10
277-280
2016
Neurospora crassa (Q7SHI8), Neurospora crassa DSM 1257 (Q7SHI8)
-
brenda
Fanuel, M.; Garajova, S.; Ropartz, D.; McGregor, N.; Brumer, H.; Rogniaux, H.; Berrin, J.G.
The Podospora anserina lytic polysaccharide monooxygenase PaLPMO9H catalyzes oxidative cleavage of diverse plant cell wall matrix glycans
Biotechnol. Biofuels
10
63
2017
Podospora anserina (B2ADG1), Podospora anserina DSM 980 (B2ADG1)
brenda
Isaksen, T.; Westereng, B.; Aachmann, F.L.; Agger, J.W.; Kracher, D.; Kittl, R.; Ludwig, R.; Haltrich, D.; Eijsink, V.G.; Horn, S.J.
A C4-oxidizing lytic polysaccharide monooxygenase cleaving both cellulose and cello-oligosaccharides
J. Biol. Chem.
289
2632-2642
2014
Neurospora crassa (Q7SHI8), Neurospora crassa, Neurospora crassa DSM 1257 (Q7SHI8)
brenda
Agger, J.W.; Isaksen, T.; Vrnai, A.; Vidal-Melgosa, S.; Willats, W.G.T.; Ludwig, R.; Horn, S.J.; Eijsink, V.G.H.; Westereng, B.
Discovery of LPMO activity on hemicelluloses shows the importance of oxidative processes in plant cell wall degradation
Proc. Natl. Acad. Sci. USA
111
6287-6292
2014
Neurospora crassa (Q7SHI8)
brenda
Courtade, G.; Wimmer, R.; R?hr, A.K.; Preims, M.; Felice, A.K.; Dimarogona, M.; Vaaje-Kolstad, G.; Sorlie, M.; Sandgren, M.; Ludwig, R.; Eijsink, V.G.; Aachmann, F.L.
Interactions of a fungal lytic polysaccharide monooxygenase with beta-glucan substrates and cellobiose dehydrogenase
Proc. Natl. Acad. Sci. USA
113
5922-5927
2016
Neurospora crassa (Q7SHI8), Neurospora crassa DSM 1257 (Q7SHI8)
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
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
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
Achaetomiella virescens, Panus similis (A0A0S2GKZ1)
brenda
Hegnar, O.A.; Petrovic, D.M.; Bissaro, B.; Alfredsen, G.; Varnai, A.; Eijsink, V.G.H.
pH-Dependent relationship between catalytic activity and hydrogen peroxide production shown via characterization of a lytic polysaccharide monooxygenase from Gloeophyllum trabeum
Appl. Environ. Microbiol.
85
e02612-18
2019
Gloeophyllum trabeum (S7RK00), Gloeophyllum trabeum ATCC 11539 (S7RK00)
brenda
Huettner, S.; Varnai, A.; Petrovic, D.; Bach, C.; Kim Anh, D.; Thanh, V.; Eijsink, V.; Larsbrink, J.; Olssona, L.
Specific xylan activity revealed for AA9 lytic polysaccharide monooxygenases of the thermophilic fungus Malbranchea cinnamomea by functional characterization
Appl. Environ. Microbiol.
85
e1408-19
2019
Malbranchea cinnamomea (A0A5J6BJT3), Malbranchea cinnamomea (A0A5J6BJT1), Malbranchea cinnamomea (A0A5J6BJN2), Malbranchea cinnamomea (A0A5J6BJQ5)
brenda
Tolgo, M.; Hegnar, O.; Ostby, H.; Varnai, A.; Vilaplana, F.; Eijsink, V.; Olsson, L.
Comparison of six lytic polysaccharide monooxygenases from Thermothielavioides terrestris shows that functional variation underlies the multiplicity of LPMO genes in filamentous fungi
Appl. Environ. Microbiol.
88
e00096
2022
Thermothielavioides terrestris (G2RGE5), Thermothielavioides terrestris (G2R6N0), Thermothielavioides terrestris (G2QZK6), Thermothielavioides terrestris ATCC 38088 (G2RGE5), Thermothielavioides terrestris ATCC 38088 (G2R6N0), Thermothielavioides terrestris ATCC 38088 (G2QZK6)
brenda
Higasi, P.M.R.; Velasco, J.A.; Pellegrini, V.O.A.; de Araujo, E.A.; Franca, B.A.; Keller, M.B.; Labate, C.A.; Blossom, B.M.; Segato, F.; Polikarpov, I.
Light-stimulated T. thermophilus two-domain LPMO9H Low-resolution SAXS model and synergy with cellulases
Carbohydr. Polym.
260
117814
2021
Thermothelomyces thermophilus
brenda
Sun, P.; de Munnik, M.; van Berkel, W.; Kabel, M.
Extending the diversity of Myceliophthora thermophila LPMOs Two different xyloglucan cleavage profiles
Carbohydr. Polym.
288
119373
2022
Thermothelomyces thermophilus
brenda
Shi, Y.; Chen, K.; Long, L.; Ding, S.
A highly xyloglucan active lytic polysaccharide monooxygenase EpLPMO9A from Eupenicillium parvum 4-14 shows boosting effect on hydrolysis of complex lignocellulosic substrates
Int. J. Biol. Macromol.
167
202-213
2021
Penicillium parvum (A0A6C0M6J9)
brenda
Petrovic, D.M.; Varnai, A.; Dimarogona, M.; Mathiesen, G.; Sandgren, M.; Westereng, B.; Eijsink, V.G.H.
Comparison of three seemingly similar lytic polysaccharide monooxygenases from Neurospora crassa suggests different roles in plant biomass degradation
J. Biol. Chem.
294
15068-15081
2019
Neurospora crassa (Q7SHI8), Neurospora crassa (Q1K8B6), Neurospora crassa (Q7S439), Neurospora crassa DSM 1257 (Q7SHI8), Neurospora crassa DSM 1257 (Q1K8B6), Neurospora crassa DSM 1257 (Q7S439)
brenda
Frandsen, K.; Haon, M.; Grisel, S.; Henrissat, B.; Leggio, L.; Berrin, J.
Identification of the molecular determinants driving the substrate specificity of fungal lytic polysaccharide monooxygenases (LPMOs)
J. Biol. Chem.
296
100086
2021
Armillaria gallica, Aspergillus fumigatus (Q4WBU0), Aspergillus fumigatus ATCC MYA-4609 (Q4WBU0), Aspergillus oryzae (Q2US83), Aspergillus oryzae ATCC 42149 (Q2US83), Bjerkandera adusta, Panus similis (A0A5S8WF95), Phanerochaete carnosa, Phanerodontia chrysosporium, Schizophyllum commune
brenda
Utarti, E.; Suwanto, A.; Thenawidjaja Suhartono, M.; Meryandini, A.
Lytic polysaccharide monooxygenase of soil actinomycete with potential use for lignocellulose biodegradation
Malay. J. Microbiol.
17
60-68
2021
Actinomyces sp.
-
brenda
Kadowaki, M.; Varnai, A.; Jameson, J.; Leite, A.; Costa-Filho, A.; Kumagai, P.; Prade, R.; Polikarpov, I.; Eijsink, V.
Functional characterization of a lytic polysaccharide monooxygenase from the thermophilic fungus Myceliophthora thermophila
PLoS ONE
13
e0202148
2018
Thermothelomyces thermophilus (G2Q7A5), Thermothelomyces thermophilus DSM 1799 (G2Q7A5)
brenda
Monclaro, A.; Petrovic, D.; Alves, G.; Costa, M.; Midorikawa, G.; Miller, R.; Filho, E.; Eijsink, V.; Varnai, A.
Characterization of two family AA9 LPMOs from Aspergillus tamarii with distinct activities on xyloglucan reveals structural differences linked to cleavage specificity
PLoS ONE
15
e0235642
2020
Aspergillus tamarii, Aspergillus tamarii CBS 117626
brenda
Petrovic, D.M.; Bissaro, B.; Chylenski, P.; Skaugen, M.; Sorlie, M.; Jensen, M.S.; Aachmann, F.L.; Courtade, G.; Varnai, A.; Eijsink, V.G.H.
Methylation of the N-terminal histidine protects a lytic polysaccharide monooxygenase from auto-oxidative inactivation
Protein Sci.
27
1636-1650
2018
Thermoascus aurantiacus (G3XAP7)
brenda
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