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Information on EC 1.14.99.56 - lytic cellulose monooxygenase (C4-dehydrogenating)
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1.14.99.56 lytic cellulose monooxygenase (C4-dehydrogenating)IUBMB Comments
This copper-containing enzyme, found in fungi and bacteria, cleaves cellulose in an oxidative manner. The cellulose fragments that are formed contain a 4-dehydro-D-glucose residue at the non-reducing end. Some enzymes also oxidize cellulose at the C-1 position of the reducing end forming a D-glucono-1,5-lactone residue [cf. EC 1.14.99.54, lytic cellulose monooxygenase (C1-hydroxylating)].
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
AA9, AA9A, Cel61a, chitin-binding domain 3 protein, FG02202.1, gh61-5, gh61e, GH61I, LPMO-02916, LPMO10B, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AA9A
FG02202.1
gh61-5
LPMO10B
LPMO9A
LPMO9C
NCU08760
Tfu_1268
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[(1->4)-beta-D-glucosyl]n+m + reduced acceptor + O2 = 4-dehydro-beta-D-glucosyl-[(1->4)-beta-D-glucosyl]n-1 + [(1->4)-beta-D-glucosyl]m + acceptor + H2O
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
cellulose, hydrogen-donor:oxygen oxidoreductase (D-glucosyl C4-dehydrogenating)
This copper-containing enzyme, found in fungi and bacteria, cleaves cellulose in an oxidative manner. The cellulose fragments that are formed contain a 4-dehydro-D-glucose residue at the non-reducing end. Some enzymes also oxidize cellulose at the C-1 position of the reducing end forming a D-glucono-1,5-lactone residue [cf. EC 1.14.99.54, lytic cellulose monooxygenase (C1-hydroxylating)].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-(1->3,1->4)-glucan + ascorbate + O2
C4-oxidized glucan oligosaccharides + dehydroascorbate + H2O
substrate is regenerated amorphous cellulose
-
-
?
cellohexaose + acceptor + O2
oxidized cellobiose and cellotriose + reduced acceptor + H2O
-
-
-
-
?
cellohexaosyl-(2-aminobenzamide) + ascorbate + O2
cellotriose + oxidized cellotriosyl-(2-aminobenzamide) + dehydroascorbate + H2O
-
-
-
-
?
cellulose + ascorbate + O2
C4-oxidized gluco-oligosaccharides + dehydroascorbate + H2O
substrate is regenerated amorphous cellulose
sole release of C4-oxidized and non-oxidized gluco-oligosaccharides
-
?
cellulose + dopamine + O2
C4-oxidized gluco-oligosaccharides + 4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O
-
dopamine shows 6% of the activity with ascorbate
-
?
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
-
-
?
konjac glucomannan + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
-
?
phosphoric acid swollen cellulose + acceptor + O2
oxidized cellobiose and cellotriose + reduced acceptor + H2O
-
-
main products, C4 is the sole site of oxidation
-
?
phosphoric acid swollen cellulose + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
-
?
phosphoric acid-swollen cellulose + ascorbate + O2
cellooligosaccharide + dehydroascorbate + H2O
-
-
-
-
?
reduced xyloglucan oligosaccharide + ascorbic acid + O2
xyloglucan oligosaccharides + dehydroascorbic acid + H2O
pure xyloglucan oligosaccharide with DP14
-
-
?
soluble beta-glucan + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
-
?
tamarind xyloglucan + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
?
xyloglucan + ascorbate + O2
C4-oxidized oligosaccharides + dehydroascorbate + H2O
-
-
-
?
avicel PH 101 + ascorbic acid + O2
? + dehydroascorbic acid + H2O
-
-
-
?
avicel PH 101 + ascorbic acid + O2
? + dehydroascorbic acid + 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
-
-
-
?
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 cellulose + ascorbate + O2
? + dehydroascorbate + H2O
-
the nonreducing end product is a 4-ketoaldose
-
?
phosphoric acid swollen cellulose + ascorbate + O2
? + dehydroascorbate + H2O
-
the nonreducing end product is a 4-ketoaldose
-
?
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
-
-
-
?
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 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: locus bean glucomannan, tamarind xyloglucan, barley beta-1,3/1,4-glucan and birchwood xylan, carboxymethylcellulose or short cellooligosaccharides
-
-
?
additional information
?
-
the enzyme inserts oxygen at the 4-position. After oxygen insertion, the glycosidic bond is destabilized and likely broken by an elimination reaction, which may be catalyzed by the PMO or occur spontaneously. This elimination is irreversible because the carbon on the reducing or nonreducing end has been oxidized
-
-
?
additional information
?
-
the enzyme inserts oxygen at the 4-position. After oxygen insertion, the glycosidic bond is destabilized and likely broken by an elimination reaction, which may be catalyzed by the PMO or occur spontaneously. This elimination is irreversible because the carbon on the reducing or nonreducing end has been oxidized
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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 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 substrates: galactan, cellopentaose, or cellohexaose
-
-
?
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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
Cu2+
Cu2+
the active site in is formed by residues His-37 and His-144 that coordinate the copper atom in a T-shaped geometry
Cu2+
-
the reduction of the mononuclear active-site copper by ascorbic acid increases the affinity and the maximum binding capacity of LPMO for cellulose
Cu2+
-
residue Tyr203 is placed approximately 15 A away from the copper active site
Cu2+
the calculated dissociation energies suggest that the reactive intermediate is either a Cu(II)-oxyl, a Cu(III)-oxyl, or a Cu(III)-hydroxide, indicating that O-O bond breaking occurs before the C-H activation step
Cu2+
enzyme is Cu(II) saturated with a 3fold molar excess of Cu(II)SO4 prior to assay
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Chlorophyllin
activity of LPMO enzymes is increased in presence of a light-driven system where photopigments such as chlorophyllin combined with a reductant donate high redox potential electrons to the LPMO. The addition of superoxide dismutase or catalase to remove reactive oxygen species does not attenuate the capacity of the light-driven LPMO system to oxidize PASC, as measured by formation of oxidized oligosaccharides
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
substrates cellulose and xyloglucan show a stabilizing effect on the apparent transition midpoint temperature of the reduced, catalytically active enzyme. Oxidative auto-inactivation and destabilization are observed in the absence of a suitable substrate
physiological function
physiological function
-
the enzyme prefers oxidation of products at C4, which lowers product binding affinity and thereby should enhance product release and processive hydrolytic turnover. Product inhibition resulting from binding of oxidized products is likely not significant
physiological function
-
isoforms LPMO9C and LPMO9F bind to nanocrystalline cellulose with high preference for the very same substrate surfaces that are also used by Hypocrea jecorina processive cellulase CBH I to move along during hydrolytic cellulose degradation. The bound LPMOs are immobile during their adsorbed residence time on cellulose. Treatment with LPMO results in fibrillation of crystalline cellulose and more than 2fold enhances the cellulase adsorption. It also increased enzyme turnover on the cellulose surface, thus boosting the hydrolytic conversion
physiological function
-
the enzyme prefers oxidation of products at C4, which lowers product binding affinity and thereby should enhance product release and processive hydrolytic turnover. Product inhibition resulting from binding of oxidized products is likely not significant
-
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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). A0A0S2GKZ1_9APHY
254
1
27138
TrEMBL
other Location (Reliability: 1)
D9SZQ3_MICAI
Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442)
366
0
38447
TrEMBL
-
I1REU9_GIBZE
Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1)
335
0
34294
TrEMBL
-
Q7RWN7_NEUCR
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
330
0
32860
TrEMBL
-
Q9RJC1_STRCO
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
228
0
25168
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
lack of potential N-glycosylation sites, presence of 37 predicted O-linked glycosylation sites. Molecular mass of recombinant protein is 75 kDa by SDS-PAGE, as compared with 32500 predicted
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
structure of AA9A bound to cellulosic and non-cellulosic oligosaccharides
substrate cellohexaose binds to subsites ?4 to +2, and cellotriose from subsites -1 to +2. Residue Tyr203 is placed approximately 15 A away from the copper active site
-
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
hybrid quantum mechanics and molecular mechanics investigation of the first steps of the LPMO mechanism, which is reduction of Cu(II) to Cu(I) and the formation of a Cu(II)-superoxide complex. In the complex, the superoxide can bind either in an equatorial or an axial position. The equatorial isomer of the superoxide complex is over 60 kJ/mol more stable than the axial isomer because it is stabilized by interactions with a second-coordination-sphere glutamine residue
comparison of isoforms LPMO9A, LPMO9B and LPMO9C. LPMO9B contains distal from the coordinated copper sphere an additional loop (Gly115-Asn121), which is not present in LPMO9A and LPMO9C. The copper ion in LPMO9A, LPMO9B and LPMO9C is coordinated by His1-His68-Tyr153, His1-His79-Tyr170 and His1-His84-Tyr166, respectively. All three LPMOs share two putative disulfide bridges
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D140A
mutant shows moderately reduced activity and essentially unchanged oxidative regioselectivity
N85F
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.9
W82Y
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 2.0
W82Y/N85F
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 10.9
W82Y/N85F/Q141W
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.1
W82Y/N85F/Y116F
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 14.7
W82Y/N85F/Y116F/Q141W
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.8
A148G
mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54
A148S
mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54
W88Y/N91F
mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54
additional information
neither truncation of the LPMO10B family 2 carbohydrate-binding module nor mutations altering access to the solvent-exposed axial copper coordination site significantly change the C1:C4 oxidation ratio
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
-
midpoint transition temperature, pH 4.0, citrate buffer, oxidized enzyme
44
-
midpoint transition temperature, pH 4.0, acetate buffer, oxidized enzyme
48.8
-
midpoint transition temperature, pH 6.0, phosphate buffer, presence of ascorbic acid
53
-
midpoint transition temperature, pH 6.0, phosphate buffer, presence of EDTA
61.5
-
midpoint transition temperature, pH 6.0, phosphate buffer, oxidized enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Aspergillus oryzae
expression in Pichia pastoris
expression in Trichoderma reesei
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
a fast, robust, and sensitive spectrophotometric activity assay based on a peroxidase activity of LPMO, using 2,6-dimethoxyphenol and H2O2. The high molar absorption coefficient of the formed Product coerulignone displays a high molar absorption coefficinet that makes the assay sensitive and allows reliable activity measurements of LPMO in concentrations of approx. 0.550 mg/L
degradation
degradation
in combination with endoglucanase and beta-glucosidase, Cel61A shows the ability to release more than 36% of the pretreated soy spent flake glucose
degradation
-
in combination with endoglucanase and beta-glucosidase, Pte6 shows the ability to release more than 36% of the pretreated soy spent flake glucose
degradation
-
lytic polysaccharide monooxygenase is able to cleave cellulose acetates with a degree of acetylation of up to 1.4
degradation
oxidative activity of Cel61A displays a synergistic effect capable of boosting endoglucanase activity, and thereby substrate depolymerization of soy cellulose, by 27%
degradation
-
the intrinsic physicochemical characteristics of Kraft pulp fibers (e.g. cellulose accessibility/degree of polymerization/crystallinity/charge) are positively enhanced by the synergistic cooperation of endoglucanase, LPMO and xylanase. LPMO addition results in the oxidative cleavage of the pulps, increasing the negative charge on the cellulose fibers, although gross fiber properties (fiber length, width and morphology) are relatively unchanged. This improves cellulose nanofibrilliation while stabilizing the nanofibril suspension, without sacrificing nanocellulose thermostability
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (A0A1C9CXI0)
brenda
Beeson, W.; Phillips, C.; Cate, J.; Marletta, M.
Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases
J. Am. Chem. Soc.
134
890-892
2012
Neurospora crassa (Q7RWN7), Neurospora crassa DSM 1257 (Q7RWN7)
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, Trichoderma reesei QM6a
brenda
Frandsen, K.E.; Simmons, T.J.; Dupree, P.; Poulsen, J.C.; Hemsworth, G.R.; Ciano, L.; Johnston, E.M.; Tovborg, M.; Johansen, K.S.; von Freiesleben, P.; Marmuse, L.; Fort, S.; Cottaz, S.; Driguez, H.; Henrissat, B.; Lenfant, N.; Tuna, F.; Baldansuren, A.; Davies, G.J.; Lo Leggio, L.; Walton, P.H.
The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases
Nat. Chem. Biol.
12
298-303
2016
Panus similis
brenda
Hedegard, E.; Ryde, U.
Multiscale modelling of lytic polysaccharide monooxygenases
ACS Omega
2
536-545
2017
Thermoascus aurantiacus (G3XAP7)
-
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)
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
Thermothielavioides terrestris (D0VWZ9)
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)
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
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)
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
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
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
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
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
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Release 2023.1 (January 2023)
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