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alpha-chitin + acceptor + O2
oligosaccharide aldonic acids + reduced acceptor + H2O
alpha-chitin + ascorbate + O2
? + dehydroascorbate + H2O
alpha-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
alpha-chitin + ascorbate + O2
chito-oligosaccharide aldonic acid + dehydroascorbate + H2O
-
products show a degree of polymerization from DP3 to DP8, with DP6 being the most abundant product after 24 h of incubation
-
?
alpha-chitin + ascorbate + O2
oxidized chitooligosaccharides + dehydroascorbate + H2O
-
-
-
?
alpha-chitin + ascorbate + O2
oxidized oligosaccharides + dehydroascorbate + H2O
beta-chitin + acceptor + O2
chito-oligosaccharide aldonic acid + reduced acceptor + H2O
-
products show a degree of polymerization from DP3 to DP8, with DP6 being the most abundant product after 24 h of incubation
-
?
beta-chitin + acceptor + O2
oligosaccharide aldonic acids + reduced acceptor + H2O
beta-chitin + ascorbate + O2
? + dehydroascorbate + H2O
beta-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
beta-chitin + ascorbate + O2
C1-oxidized oligosaccharides + dehydroascorbate + H2O
beta-chitin + ascorbate + O2
oxidized oligosaccharides + dehydroascorbate + H2O
beta-chitin + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
-
?
beta-chitin + cellobiose dehydrogenase + O2
C1-oxidized oligosaccharides + reduced cellobiose dehydrogenase + H2O
chitin + acceptor + O2
? + reduced acceptor + H2O
-
-
-
?
chitin + acceptor + O2
C1-oxidized chito-oligosaccharides + reduced acceptor + H2O
chitin + acceptor + O2
[chitin oligosaccharide]-N-acetyl-D-glucosaminate + [chitin oligosaccharide]-N-acetyl-D-glucosamino-1,5-lactone
chitin + ascorbic acid + O2
? + dehydroascorbate + H2O
colloidal chitin + ascorbate + O2
? + dehydroascorbate + H2O
colloidal chitin + ascorbate + O2
oxidized chitin oligosaccharides + dehydroascorbate + H2O
colloidal chitin + ascorbate + O2
[chitin oligosaccharide]-N-acetyl-D-glucosaminate + [chitin oligosaccharide]-N-acetyl-D-glucosamino-1,5-lactone + dehydroascorbate + H2O
crystalline chitin + ascorbate + O2
oxidized oligosaccharides + dehydroascorbate + H2O
phosphoric acid swollen cellulase + ascorbic acid + O2
? + dehydroascorbate + H2O
phosphoric acid swollen cellulose + ascorbate + O2
C4-oxidized cellooligosaccharides + C1/C4-oxidized cellooligosaccharides + dehydroascorbate + H2O
reaction of EC 1.14.99.54
-
-
?
[(1->4)-N-acetyl-beta-D-glucosaminyl]6 + ascorbate + O2
[(1->4)-N-acetyl-beta-D-glucosaminyl]3-(1->4)-N-acetyl-2-deoxy-2-amino-D-glucono-1,5-lactone + [(1->4)-N-acetyl-beta-D-glucosaminyl]2 + dehydroascorbate + H2O
-
-
-
?
[(1->4)-N-acetyl-beta-D-glucosaminyl]n+m + reduced acceptor + O2
[(1->4)-N-acetyl-beta-D-glucosaminyl]m-1-(1->4)-N-acetyl-2-deoxy-2-amino-D-glucono-1,5-lactone + [(1->4)-N-acetyl-beta-D-glucosaminyl]n + acceptor + H2O
additional information
?
-
alpha-chitin + acceptor + O2
oligosaccharide aldonic acids + reduced acceptor + H2O
-
-
-
-
?
alpha-chitin + acceptor + O2
oligosaccharide aldonic acids + reduced acceptor + H2O
-
-
-
-
?
alpha-chitin + ascorbate + O2
? + dehydroascorbate + H2O
-
products are the aldonic acid forms of fully acetylated chitooligosaccharides, oxidation occurs at the C1 carbon atom
-
?
alpha-chitin + ascorbate + O2
? + dehydroascorbate + H2O
-
products are the aldonic acid forms of fully acetylated chitooligosaccharides, oxidation occurs at the C1 carbon atom
-
?
alpha-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
-
products are C1-oxidized chitooligomers, mainly tetramers and hexamers
-
?
alpha-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
-
products are C1-oxidized chitooligomers, mainly tetramers and hexamers
-
?
alpha-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
enzyme shows stronger binding and a greater release of soluble oxidized products with beta-chitin than with alpha-chitin
products show oxidation of the C1 carbon leading to aldonic acids
-
?
alpha-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
enzyme shows stronger binding and a greater release of soluble oxidized products with beta-chitin than with alpha-chitin
products show oxidation of the C1 carbon leading to aldonic acids
-
?
alpha-chitin + ascorbate + O2
oxidized oligosaccharides + dehydroascorbate + H2O
-
-
-
?
alpha-chitin + ascorbate + O2
oxidized oligosaccharides + dehydroascorbate + H2O
-
-
-
?
beta-chitin + acceptor + O2
oligosaccharide aldonic acids + reduced acceptor + H2O
-
beta chitin from squid pen, best substrate
strong preference towards even-numbered products
-
?
beta-chitin + acceptor + O2
oligosaccharide aldonic acids + reduced acceptor + H2O
-
beta chitin from squid pen, best substrate
strong preference towards even-numbered products
-
?
beta-chitin + ascorbate + O2
? + dehydroascorbate + H2O
-
products are the aldonic acid forms of fully acetylated chitooligosaccharides, oxidation occurs at the C1 carbon atom
-
?
beta-chitin + ascorbate + O2
? + dehydroascorbate + H2O
-
products are the aldonic acid forms of fully acetylated chitooligosaccharides, oxidation occurs at the C1 carbon atom
-
?
beta-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
beta-chitin is preferred over alpha-chitin
products are C1-oxidized chitooligomers, mainly tetramers and hexamers
-
?
beta-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
beta-chitin is preferred over alpha-chitin
products are C1-oxidized chitooligomers, mainly tetramers and hexamers
-
?
beta-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
-
-
-
?
beta-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
enzyme shows stronger binding and a greater release of soluble oxidized products with beta-chitin than with alpha-chitin
products show oxidation of the C1 carbon leading mainly to tetrameric and hexameric aldonic acids
-
?
beta-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
enzyme shows stronger binding and a greater release of soluble oxidized products with beta-chitin than with alpha-chitin
products show oxidation of the C1 carbon leading mainly to tetrameric and hexameric aldonic acids
-
?
beta-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
-
-
-
-
?
beta-chitin + ascorbate + O2
C1-oxidized oligosaccharides + dehydroascorbate + H2O
-
-
-
?
beta-chitin + ascorbate + O2
C1-oxidized oligosaccharides + dehydroascorbate + H2O
substrate squid pen beta-chitin
in addition, considerable amounts of partially deacetylated oligomers are produced
-
?
beta-chitin + ascorbate + O2
C1-oxidized oligosaccharides + dehydroascorbate + H2O
substrate squid pen beta-chitin
in addition, considerable amounts of partially deacetylated oligomers are produced
-
?
beta-chitin + ascorbate + O2
C1-oxidized oligosaccharides + dehydroascorbate + H2O
-
-
-
?
beta-chitin + ascorbate + O2
oxidized oligosaccharides + dehydroascorbate + H2O
-
-
-
?
beta-chitin + ascorbate + O2
oxidized oligosaccharides + dehydroascorbate + H2O
-
-
-
?
beta-chitin + cellobiose dehydrogenase + O2
C1-oxidized oligosaccharides + reduced cellobiose dehydrogenase + H2O
cellobiose dehydrogenase from Myriococcum thermophilum can act as an electron donor
-
-
?
beta-chitin + cellobiose dehydrogenase + O2
C1-oxidized oligosaccharides + reduced cellobiose dehydrogenase + H2O
cellobiose dehydrogenase from Myriococcum thermophilum can act as an electron donor
-
-
?
chitin + acceptor + O2
C1-oxidized chito-oligosaccharides + reduced acceptor + H2O
-
primary chain cleavage, yielding predominantly aldonic acid oligosaccharides with even-numbered degrees of polymerization plus significant presence of unmodified oligosaccharides with uneven-numbered degrees of polymerization
-
?
chitin + acceptor + O2
C1-oxidized chito-oligosaccharides + reduced acceptor + H2O
-
primary chain cleavage, yielding predominantly aldonic acid oligosaccharides with even-numbered degrees of polymerization plus significant presence of unmodified oligosaccharides with uneven-numbered degrees of polymerization
-
?
chitin + acceptor + O2
[chitin oligosaccharide]-N-acetyl-D-glucosaminate + [chitin oligosaccharide]-N-acetyl-D-glucosamino-1,5-lactone
-
the products are a series of chitin oligosaccharides in aldonic acid or lactone form with varying degree of polymerization: DPox4 > DPox5 > DPox6 > DPox7 > DPox8. Oligosaccharides with even-numbered chain lengths are predominant.
-
?
chitin + acceptor + O2
[chitin oligosaccharide]-N-acetyl-D-glucosaminate + [chitin oligosaccharide]-N-acetyl-D-glucosamino-1,5-lactone
-
the products are a series of chitin oligosaccharides in aldonic acid or lactone form with varying degree of polymerization: DPox4 > DPox5 > DPox6 > DPox7 > DPox8. Oligosaccharides with even-numbered chain lengths are predominant.
-
?
chitin + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
?
chitin + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
?
chitin + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
?
chitin + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
?
colloidal chitin + ascorbate + O2
? + dehydroascorbate + H2O
-
low activity, products show less dominance of even-numbered products than alpha- or beta-chitin
-
?
colloidal chitin + ascorbate + O2
? + dehydroascorbate + H2O
-
low activity, products show less dominance of even-numbered products than alpha- or beta-chitin
-
?
colloidal chitin + ascorbate + O2
oxidized chitin oligosaccharides + dehydroascorbate + H2O
-
with colloidal chitin as the substrate, a ladder of oxidized oligosaccharides is observed
-
?
colloidal chitin + ascorbate + O2
oxidized chitin oligosaccharides + dehydroascorbate + H2O
-
with colloidal chitin as the substrate, a ladder of oxidized oligosaccharides is observed
-
?
colloidal chitin + ascorbate + O2
[chitin oligosaccharide]-N-acetyl-D-glucosaminate + [chitin oligosaccharide]-N-acetyl-D-glucosamino-1,5-lactone + dehydroascorbate + H2O
-
-
-
?
colloidal chitin + ascorbate + O2
[chitin oligosaccharide]-N-acetyl-D-glucosaminate + [chitin oligosaccharide]-N-acetyl-D-glucosamino-1,5-lactone + dehydroascorbate + H2O
-
-
-
?
crystalline chitin + ascorbate + O2
oxidized oligosaccharides + dehydroascorbate + H2O
-
enzyme generates even-numbered oxidized oligosaccharides as the dominated products from crystalline chitin
-
?
crystalline chitin + ascorbate + O2
oxidized oligosaccharides + dehydroascorbate + H2O
-
enzyme generates even-numbered oxidized oligosaccharides as the dominated products from crystalline chitin
-
?
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
-
-
-
?
[(1->4)-N-acetyl-beta-D-glucosaminyl]n+m + reduced acceptor + O2
[(1->4)-N-acetyl-beta-D-glucosaminyl]m-1-(1->4)-N-acetyl-2-deoxy-2-amino-D-glucono-1,5-lactone + [(1->4)-N-acetyl-beta-D-glucosaminyl]n + acceptor + H2O
-
-
-
?
[(1->4)-N-acetyl-beta-D-glucosaminyl]n+m + reduced acceptor + O2
[(1->4)-N-acetyl-beta-D-glucosaminyl]m-1-(1->4)-N-acetyl-2-deoxy-2-amino-D-glucono-1,5-lactone + [(1->4)-N-acetyl-beta-D-glucosaminyl]n + acceptor + H2O
-
-
-
?
additional information
?
-
no activity on other substrates including diverse mannans, cellulose and starch
-
-
?
additional information
?
-
no activity on other substrates including diverse mannans, cellulose and starch
-
-
?
additional information
?
-
the enzyme produces oxidized chitin oligosaccharides with a degree of polymerization from DPox3 to DPox11. The relative intensities of DPox4, DPox6, DPox8 and DPox10 are remarkably higher than DPox5, DPox7, DPox9 and DPox11. LPMO10A shows little binding to Avicel
-
-
?
additional information
?
-
the enzyme produces oxidized chitin oligosaccharides with a degree of polymerization from DPox3 to DPox11. The relative intensities of DPox4, DPox6, DPox8 and DPox10 are remarkably higher than DPox5, DPox7, DPox9 and DPox11. LPMO10A shows little binding to Avicel
-
-
?
additional information
?
-
data indicate that catalysis involves equatorial binding of a reactive oxygen species
-
-
?
additional information
?
-
the enzyme is active on alpha- and beta-chitin, and the chitin-binding surface previously described for larger LPMOs is fully conserved
-
-
?
additional information
?
-
data indicate that catalysis involves equatorial binding of a reactive oxygen species
-
-
?
additional information
?
-
the enzyme is active on alpha- and beta-chitin, and the chitin-binding surface previously described for larger LPMOs is fully conserved
-
-
?
additional information
?
-
enzyme binds to cellulose, but does not display catalyic activity
-
-
?
additional information
?
-
enzyme binds to cellulose, but does not display catalyic activity
-
-
?
additional information
?
-
mechanistic model, copper is reduced on the enzyme by an externally provided electron and followed by oxygen binding and activation by internal electron transfer. Substrate binding involves an extended planar binding surface, including the metal binding site. Chitin binding protects two regions from 2H/1H exchange, Gln53-Ser58 and Leu110-Thr116
-
-
?
additional information
?
-
[(1->4)-N-acetyl-beta-D-glucosaminyl]6 is a substrate, but not shorter oligomers
-
-
?
additional information
?
-
enzyme in presence of ascorbate but lacking chitin produces H2O2
-
-
?
additional information
?
-
isoform LPMO10B produces C4-oxidized (4-ketoaldoses) and double (C4/C1)-oxidized cello-oligosaccharides. No substrate: alpha-chitin
-
-
?
additional information
?
-
isoform LPMO10B produces C4-oxidized (4-ketoaldoses) and double (C4/C1)-oxidized cello-oligosaccharides. No substrate: alpha-chitin
-
-
?
additional information
?
-
enzyme in presence of ascorbate but lacking chitin produces H2O2
-
-
?
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in presence of Zn2+, to 1.55 A resolution, and in presence of Cu2+, to 1.4 AS resolution
analysis of the copper active site
-
comparative analysis of sequences, solved structures, and homology models from AA9 and AA10 LPMO families.The two LPMO families are highly conserved, structurally they have minimal sequence similarity outside the active site residues
to 1.85 A resolution, tri-modular enzyme containing a catalytic family AA10 LPMO module, a family 5 chitin-binding module, and a C-terminal unclassified module which displays tight and specific binding to chitin
comparative analysis of sequences, solved structures, and homology models from AA9 and AA10 LPMO families.The two LPMO families are highly conserved, structurally they have minimal sequence similarity outside the active site residues
crystal structure in the Cu(II)-bound form and photoreduction of the crystalline protein in the x-ray beam, leading to conversion from the initial Cu(II)-oxidized form with two coordinated water molecules, which adopts a trigonal bipyramidal geometry, to a reduced Cu(I) form in a T-shaped geometry with no coordinated water molecules
1.1 A resolution room-temperature X-ray structure and 2.1 A resolution neutron structure, show a putative dioxygen species equatorially bound to the active site copper with elongated density for the dioxygen, most consistent with a Cu(II)-bound peroxide
1.1 A resolution, room-temperature X-ray structure and a 2.1 A resolution neutron structure show a putative dioxygen species equatorially bound to the active site copper. Both structures show an elongated density for the dioxygen, consistent with a Cu(II)-bound peroxide. The coordination environment is consistent with Cu(II). The N-terminal amino group, involved in copper coordination, is present as a mixed neutral and deprotonated form
1.55 A resolution structure of N-terminal LPMO10A module reveals deletions of interacting loops that protrude from the core beta-sandwich scaffold in larger LPMO10s
structure of the catalytic domain, residues 37-230, to 1.08 A resolution. The active site in is formed by residues His-37 and His-144 that coordinate the copper atom in a T-shaped geometry
structures in the resting state and of a copper(II)-dioxo intermediate complex formed in the absence of substrate reveal pre-bound molecular oxygen adjacent to the active site. A conserved histidine is involved in promoting oxygen activation
to 1.2 A resolution. Diffraction resolution and crystal morphology are improved by expression from a glycoengineered strain of Pichia pastoris
crystallization at pH 3.5. Structure shows shows significant disorder of the active site in the absence of substrate ligand
calculation of solution structure. Ca2+, Mg2+, Fe3+, Co2+, Zn2+, or Cu2+ ions show binding to an interaction site located between His28 and His114
molecular dynamics interactions between the LPMO and three different surface topologies of crystalline chitin. Most enzyme-substrate interactions involve the polysaccharide chain that is to be cleaved. Enzyme displays a constrained active site geometry as well as a tunnel connecting the bulk solvent to the copper site, through which only small molecules such as H2O, O2, and H2O2 can diffuse. Rearrangement of Cu-coordinating water molecules is necessary when binding the substrate and also provide a rationale for the experimentally observed C1 oxidative regiospecificity
structure of the catalytic domain, residues 37-230, to 1.08 A resolution. The active site in is formed by residues His-37 and His-144 that coordinate the copper atom in a T-shaped geometry
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Duzhak, A.B.; Panfilova, Z.I.; Duzhak, T.G.; Vasyunina, E.A.
Extracellular chitinases of mutant superproducing strain Serratia marcescens M-1
Biochemistry (Moscow)
74
209-214
2009
Serratia marcescens (O83009)
brenda
Zhang, H.; Zhao, Y.; Cao, H.; Mou, G.; Yin, H.
Expression and characterization of a lytic polysaccharide monooxygenase from Bacillus thuringiensis
Int. J. Biol. Macromol.
79
72-75
2015
Bacillus thuringiensis (A0A0C5K362), Bacillus thuringiensis serovar kurstaki (A0A0C5K362), Bacillus thuringiensis ACCC 10066 (A0A0C5K362), Bacillus thuringiensis serovar kurstaki ACCC 10066 (A0A0C5K362)
brenda
Gudmundsson, M.; Kim, S.; Wu, M.; Ishida, T.; Momeni, M.H.; Vaaje-Kolstad, G.; Lundberg, D.; Royant, A.; Stahlberg, J.; Eijsink, V.G.; Beckham, G.T.; Sandgren, M.
Structural and electronic snapshots during the transition from a Cu(II) to Cu(I) metal center of a lytic polysaccharide monooxygenase by X-ray photoreduction
J. Biol. Chem.
289
18782-18792
2014
Enterococcus faecalis (Q838S1)
brenda
Vaaje-Kolstad, G.; Bohle, L.A.; Gaseidnes, S.; Dalhus, B.; Bjoras, M.; Mathiesen, G.; Eijsink, V.G.
Characterization of the chitinolytic machinery of Enterococcus faecalis V583 and high-resolution structure of its oxidative CBM33 enzyme
J. Mol. Biol.
416
239-254
2012
Enterococcus faecalis (Q838S1)
brenda
Vaaje-Kolstad, G.; Westereng, B.; Horn, S.J.; Liu, Z.; Zhai, H.; Sorlie, M.; Eijsink, V.G.
An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides
Science
330
219-222
2010
Serratia marcescens (O83009)
brenda
Bacik, J.P.; Mekasha, S.; Forsberg, Z.; Kovalevsky, A.Y.; Vaaje-Kolstad, G.; Eijsink, V.G.H.; Nix, J.C.; Coates, L.; Cuneo, M.J.; Unkefer, C.J.; Chen, J.C.
Neutron and atomic resolution X-ray structures of a lytic polysaccharide monooxygenase reveal copper-mediated dioxygen binding and evidence for N-terminal deprotonation
Biochemistry
56
2529-2532
2017
Jonesia denitrificans (C7R4I0), Jonesia denitrificans DSM 20603 (C7R4I0)
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
Burkholderia pseudomallei (Q3JY22), Enterococcus faecalis (Q838S1), Enterococcus faecalis ATCC 700802 (Q838S1), Burkholderia pseudomallei 1710b (Q3JY22)
brenda
Hamre, A.G.; Eide, K.B.; Wold, H.H.; Sorlie, M.
Activation of enzymatic chitin degradation by a lytic polysaccharide monooxygenase
Carbohydr. Res.
407
166-169
2015
Serratia marcescens (O83009)
brenda
Gregory, R.C.; Hemsworth, G.R.; Turkenburg, J.P.; Hart, S.J.; Walton, P.H.; Davies, G.J.
Activity, stability and 3-D structure of the Cu(II) form of a chitin-active lytic polysaccharide monooxygenase from Bacillus amyloliquefaciens
Dalton Trans.
45
16904-16912
2016
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens DSM 7
brenda
Yu, M.J.; Yoon, S.H.; Kim, Y.W.
Overproduction and characterization of a lytic polysaccharide monooxygenase in Bacillus subtilis using an assay based on ascorbate consumption
Enzyme Microb. Technol.
93-94
150-156
2016
Bacillus atrophaeus (A0A0H3E2X6), Bacillus atrophaeus 1942 (A0A0H3E2X6)
brenda
Nakagawa, Y.S.; Kudo, M.; Loose, J.S.; Ishikawa, T.; Totani, K.; Eijsink, V.G.; Vaaje-Kolstad, G.
A small lytic polysaccharide monooxygenase from Streptomyces griseus targeting alpha- and beta-chitin
FEBS J.
282
1065-1079
2015
Streptomyces griseus subsp. griseus (B1VN59), Streptomyces griseus subsp. griseus JCM 4626 (B1VN59)
brenda
Paspaliari, D.K.; Loose, J.S.; Larsen, M.H.; Vaaje-Kolstad, G.
Listeria monocytogenes has a functional chitinolytic system and an active lytic polysaccharide monooxygenase
FEBS J.
282
921-936
2015
Listeria monocytogenes serotype 1/2a (Q8Y4H4), Listeria monocytogenes serotype 1/2a ATCC BAA-679 (Q8Y4H4)
brenda
Loose, J.; Forsberg, Z.; Fraaije, M.; Eijsink, V.; Vaaje-Kolstad, G.
A rapid quantitative activity assay shows that the Vibrio cholerae colonization factor GbpA is an active lytic polysaccharide monooxygenase
FEBS Lett.
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Aspergillus oryzae (Q2UA85), Aspergillus oryzae ATCC 42149 (Q2UA85)
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Neutron and atomic resolution X-ray structures of a lytic polysaccharide monooxygenase reveal copper-mediated dioxygen binding and evidence for N-terminal deprotonation
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Jonesia denitrificans (C7R4I0), Jonesia denitrificans DSM 20603 (C7R4I0)
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How a lytic polysaccharide monooxygenase binds crystalline chitin
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Serratia marcescens (O83009)
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Frandsen, K.; Poulsen, J.; Tandrup, T.; Lo Leggio, L.
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