Information on EC 1.14.99.54 - lytic cellulose monooxygenase (C1-hydroxylating)

for references in articles please use BRENDA:EC1.14.99.54
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.14.99.54
-
RECOMMENDED NAME
GeneOntology No.
lytic cellulose monooxygenase (C1-hydroxylating)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[(1->4)-beta-D-glucosyl]n+m + reduced acceptor + O2 = [(1->4)-beta-D-glucosyl]m-1-(1->4)-D-glucono-1,5-lactone + [(1->4)-beta-D-glucosyl]n + acceptor + H2O
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
cellulose, hydrogen-donor:oxygen oxidoreductase (D-glucosyl C1-hydroxylating)
This copper-containing enzyme, found in fungi and bacteria, cleaves cellulose in an oxidative manner. The cellulose fragments that are formed contain a D-glucono-1,5-lactone residue at the reducing end, which hydrolyses quickly and spontaneously to the aldonic acid. The electrons are provided in vivo by the cytochrome b domain of EC 1.1.99.18, cellobiose dehydrogenase (acceptor) [1]. Ascorbate can serve as the electron donor in vitro.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
mangrove-associated fungus
KR825269, KR825270
Genbank
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
Thielavia heterothallica
UniProt
Manually annotated by BRENDA team
Thielavia heterothallica
UniProt
Manually annotated by BRENDA team
-
D0VWZ9
UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,6-dimethoxyphenol + 2 H2O2
coerulignone + 2 H2O
show the reaction diagram
-
-
-
-
?
amorphous cellulose + 2 AH2 + 2 O2
cellooligosaccharide-C6-aldehyde-C1-lactone + 2 A + 2 H2O
show the reaction diagram
amorphous cellulose + AH2 + O2
cellooligosaccharide-C1-lactone + A + H2O
show the reaction diagram
avicel + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
avicel + ascorbate + O2
C1-oxidized oligosaccharides + dehydroascorbate + H2O
show the reaction diagram
avicel + ascorbate + O2
C4-oxidized oligosaccharides + C1/C4-oxidized oligosaccharides + dehydroascorbate + H2O
show the reaction diagram
avicel + ascorbic acid + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
avicel + ascorbic acid + O2
? + dehydroascorbic acid + H2O
show the reaction diagram
-
-
-
-
?
avicel PH 101 + ascorbic acid + O2
? + dehydroascorbic acid + H2O
show the reaction diagram
bacterial microcrystalline cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
show the reaction diagram
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individual AA9A molecules exhibit intermittent random movement along, across, and penetrating into the ribbon-like microfibril structure of bacterial microcrystalline cellulose, concomitant with the release of a small amount of oxidized sugars and the splitting of large cellulose ribbons into fibrils with smaller diameters
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-
?
beta-(1->3,1->4)-glucan + acceptor + O2
C1/C4-oxidized oxidized glucan oligosaccharides + reduced acceptor + H2O
show the reaction diagram
-
-
-
?
beta-chitin + ascorbate + O2
C4-oxidized oligosaccharides + C1/C4-oxidized oligosaccharides + dehydroascorbate + H2O
show the reaction diagram
birchwood cellulose + ascorbic acid + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
cellohexaosyl-(2-aminobenzamide) + ascorbate + O2
cellotriose + oxidized cellotriosyl-(2-aminobenzamide) + dehydroascorbate + H2O
show the reaction diagram
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-
-
?
cellooligosaccharide + pyrogallol + O2
-
show the reaction diagram
-
-
-
?
cellulose + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
cellulose + ascorbate + O2
C1-oxidized cellooligosaccharides + dehydroascorbate + H2O
show the reaction diagram
cellulose + ascorbate + O2
C1-oxidized glucooligosaccharides + glucooligosaccharides + dehydroascorbate + H2O
show the reaction diagram
substrate is regenerated amorphous cellulose
release of C1-oxidized and non-oxidized glucooligosaccharides
-
?
cellulose + ascorbate + O2
C1/C4-oxidized cello-oligosaccharides + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
cellulose + ascorbate + O2
C1/C4-oxidized cellooligosaccharides + cellooligosaccharides + dehydroascorbate + H2O
show the reaction diagram
substrate regenerated amorphous cellulose
enzyme cleaves beta-(1->4)-glucosyl bonds in cellulose under formation of oxidized gluco-oligosaccharides. Both C1 and C4 oxidized gluco-oligosaccharides and non-oxidized gluco-oligosaccharides are formed
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?
cellulose + ascorbate + O2
C1/C4-oxidized cellooligosaccharides + dehydroascorbate + H2O
show the reaction diagram
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enzyme oxidizes cellulose at both the C1 and C4 positions
-
?
cellulose + ascorbic acid + O2
? + dehydroascorbate + H2O
show the reaction diagram
cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
show the reaction diagram
-
-
-
-
?
cellulose + oxidized dopamine + O2
C1-oxidized gluco-oligosaccharides + glucooligosaccharides + dopamine + H2O
show the reaction diagram
-
dopamine shows 46% of the activity with ascorbate
-
?
cellulose + reduced acceptor + O2
? + oxidized acceptor + H2O
show the reaction diagram
-
-
-
-
?
cellulose acetate + ? + O2
? + H2O
show the reaction diagram
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lytic polysaccharide monooxygenase is able to cleave cellulose acetates with a degree of acetylation of up to 1.4. Preferentially, fragments with a low degree of acetylation are released
-
-
?
chitin + ascorbic acid + O2
? + dehydroascorbate + H2O
show the reaction diagram
filter paper + ascorbic acid + O2
? + dehydroascorbate + H2O
show the reaction diagram
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-
-
-
?
filter paper + ascorbic acid + O2
? + dehydroascorbic acid + H2O
show the reaction diagram
Kraft pulp + gallate + O2
? + H2O
show the reaction diagram
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-
-
-
?
microcrystalline cellulose + AH2 + O2
?
show the reaction diagram
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enzyme catalyzes release of a mixture of soluble sugars comprising reduced and oxidized cellooligosaccharides. The degree of polymerization of the released oligosaccharides ranges from 3 to 5 for the reduced products and from 2 to 5 for the oxidized products
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?
NaOH pretreated soy spent flakes + ascorbic acid + O2
? + dehydroascorbic acid + H2O
show the reaction diagram
NaOH-treated soy spent flake + ascorbate + O2
C1/C4-oxidized cellooligosaccharides + dehydroascorbate + H2O
show the reaction diagram
-
native soy spentflake is not a substrate
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?
phosphoric acid swollen cellulase + ascorbic acid + O2
? + dehydroascorbate + H2O
show the reaction diagram
phosphoric acid swollen cellulose + AH2 + O2
? + dehydroascorbate + H2O
show the reaction diagram
phosphoric acid swollen cellulose + ascorbate + O2
C1-oxidized cellooligosaccharides + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
phosphoric acid swollen cellulose + ascorbate + O2
C1-oxidized oligosaccharides + dehydroascorbate + H2O
show the reaction diagram
phosphoric acid swollen cellulose + ascorbate + O2
C1/C4-oxidized cellooligosaccharides + dehydroascorbate + H2O
show the reaction diagram
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enzyme oxidizes cellulose at both the C1 and C4 positions
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?
phosphoric acid swollen cellulose + ascorbate + O2
C4-dehydro-cellooligosaccharide + dehydroascorbate + 2 H2O
show the reaction diagram
KR825269;, KR825270;
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The chain lengths of the cellooligosaccharides ranges from 2 to 5
-
?
phosphoric acid swollen cellulose + ascorbate + O2
C4-dehydro-cellooligosaccharide-C1-lactone + dehydroascorbate + H2O
show the reaction diagram
KR825269;, KR825270;
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the initially formed lactone at the reducing end of the produced cellooligosaccharides is hydrolyzed spontanously to the aldonic acid. The chain lengths of the cellooligosaccharides ranges from 2 to 5
-
?
phosphoric acid swollen cellulose + ascorbate + O2
cellooligosaccharide-C1-lactone + dehydroascorbate + H2O
show the reaction diagram
KR825269;, KR825270;
-
the initially formed lactone at the reducing end of the produced cellooligosaccharides is hydrolyzed spontanously to the aldonic acid. The chain lengths of the cellooligosaccharides ranges from 2 to 5
-
?
phosphoric acid swollen cellulose + ascorbate + O2
oxidized oligosaccharides + dehydroascorbate + H2O
show the reaction diagram
phosphoric acid swollen cellulose + ascorbic acid + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
phosphoric acid swollen cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
show the reaction diagram
phosphoric acid swollen cellulose + ascorbic acid + O2
cellobionic acid + ? + dehydroascorbate + H2O
show the reaction diagram
phosphoric acid-swollen cellulose + ascorbate + O2
cellooligosaccharide + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
regenerated amorphous cellulose + 3-methylcatechol + O2
3-methyl-o-benzoquinone + H2O
show the reaction diagram
-
-
-
?
regenerated amorphous cellulose + 3-methylcatechol + O2
? + 3-methyl-o-benzoquinone + H2O
show the reaction diagram
-
-
-
?
regenerated amorphous cellulose + ascorbic acid + O2
? + dehydroascorbic acid + H2O
show the reaction diagram
-
-
-
?
regenerated amorphous cellulose + ascorbic acid + O2
dehydroascorbic acid + H2O
show the reaction diagram
-
-
-
?
soluble beta-glucan + ascorbic acid + O2
? + dehydroascorbic acid + H2O
show the reaction diagram
-
-
-
-
?
steam-exploded spruce + ascorbate + O2
C1-oxidized cellooligosaccharides + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
tamarind xyloglucan + ascorbic acid + O2
? + dehydroascorbic acid + H2O
show the reaction diagram
xylan + dopamine + O2
C1/C4-oxidized oxidized xylo-oligosaccharides + 4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O
show the reaction diagram
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93% of the activiy with ascorbate
-
?
xylan + dopamine + O2
C1/C4-oxidized xylooligosaccharides + 4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O
show the reaction diagram
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enzyme cleaves beta-(1->4)-xylosyl bonds in xylan under formation of oxidized xylo-oligosaccharides
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?
xyloglucan + acceptor + O2
C1/C4-oxidized oxidized oligosaccharides + reduced acceptor + H2O
show the reaction diagram
-
-
-
?
xyloglucan + ascorbate + O2
?
show the reaction diagram
xyloglucanoligosaccharide + ascorbic acid + O2
xyloglucan oligosaccharide + dehydroascorbic acid + H2O
show the reaction diagram
[(1->4)-beta-D-glucosyl]n+m + AH2 + O2
[(1->4)-beta-D-glucosyl]m-1-(1->4)-D-glucono-1,5-lactone + [(1->4)-beta-D-glucosyl]n + A + H2O
show the reaction diagram
[(1->4)-beta-D-xylosyl]6-(1->4)-beta-D-glucose + ascorbate + O2
?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[(1->4)-beta-D-glucosyl]n+m + AH2 + O2
[(1->4)-beta-D-glucosyl]m-1-(1->4)-D-glucono-1,5-lactone + [(1->4)-beta-D-glucosyl]n + A + H2O
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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2 mM, complete loss of activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cellobiose dehydrogenase
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Chlorophyllin
Cu2+
-
the copper ion lies in an octahedral environment exhibiting Jahn-Teller distortion; the copper ion lies in an octahedral environment exhibiting Jahn-Teller distortion
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015 - 0.021
cellulose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8
assay at; assay at
5.5
KR825269;, KR825270;
;
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 5
hardly any catalytic performance at a low pH
5 - 6.5
KR825269;, KR825270;
no activity below pH 4.5; no activity below pH 4.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
optimum in presence of 3-methylcatechol; optimum in presence of ascorbic acid
45
assay at; assay at
50 - 60
optimum in presence of 3-methylcatechol
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
methylation
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals obtained in the presence of high zinc-ion concentrations are used. A structure with an ordered zinc-bound active site at 1.65 A resolution, and three structures from crystals soaked with maltooligosaccharides in solutions devoid of zinc ions are solved at resolutions of up to 1.10 A
structure determined at pH 3.5, shows significant disorder of the active site in the absence of substrate ligand
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structure of AA9A bound to cellulosic and non-cellulosic oligosaccharides
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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
1.2 A resolution X-ray diffraction data, room-temperature neutron diffraction data to 2.12 A resolution
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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; 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
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comparison of isoforms PMO-2 and PMO-3 at 1.1 and 1.37 resolution, respectively. In the structures, dioxygen species are found in the active sites. The enzyme substrate-binding surfaces contain highly varied aromatic amino acid and glycosylation positions; comparison of isoforms PMO-2 and PMO-3 at 1.1 and 1.37 resolution, respectively. In the structures, dioxygen species are found in the active sites. The enzyme substrate-binding surfaces contain highly varied aromatic amino acid and glycosylation positions
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single-molecule study by atomic force microscopy
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to 1.2 A resolution, P21 space group with two protein molecules with non-crystallographic symmetry per asymmetric unit. Role for a conserved histidine in promoting oxygen activation
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to 1.75 A resolution. Stucture reveals a copper-bound active site common to LPMOs, a collection of aromatic and polar residues near the binding surface that may be responsible for regioselectivity, and substantial differences in loop structures near the binding face. Surface analysis reveals energy wells whose spacing seems adapted to the spacing of cellobiose units along a cellulose chain
to 3.0 A resolution. The active site of AA14B is constituted by His1, His99 and Tyr176, forming the canonical histidine brace that is exposed at the surface
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
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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to 1.3 A resolution; to 1.3 A resolution
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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
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hybrid quantum mechanics and molecular mechanics investigation of the first steps of the LPMO mechanism, which is reduction of CuII to CuI and the formation of a CuII-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; 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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modeling of structure. The divalent metal ion in the active site is coordinated by the three amino acids, His1, His68 and Tyr153. LPMO9A comprises two disulfide bridges, Cys126-Cys208 and Cys38-Cys156
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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
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C-terminally truncated variant containing 21 residues of the predicted linker domain, to 0.95 A resolution. The linker forms an integral part of the catalytic domain structure, covering a hydrophobic patch on the catalytic AA9 module. The oxidized catalytic center contains a Cu(II) coordinated by two His ligands, one of which has a His-brace in which the His-1 terminal amine group also coordinates to a copper. The final equatorial position of the Cu(II) is occupied by a water-derived ligand
G0R6T8;
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
inactivation within the first 6 h at pH values above 6
744131
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 40
KR825269;, KR825270;
100% activity after 150 min and approximately 80% after 1000 min of incubation; 100% activity after 150 min and approximately 80% after 1000 min of incubation
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nickel chelate His-bind resin column chomatography; nickel chelate His-bind resin column chomatography
simple purification method by affinity adsorption to obtain functional lytic polysaccharide monooxygenases. Purification follows a binding-elution protocol with low-grade polysaccharides including Avicel
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed and produced in a protease/(hemi-) cellulase-free Myceliophthora thermophila C1 strain
expressed in Pichia pastoris; expressed in Pichia pastoris
expression in Aspergillus oryzae
expression in Escherichia coli
expression in Escherichia coli and Pichia pastoris
expression in glycoengineered Pichia pastoris
-
expression in Hypocrea jecorina
G0R6T8;
expression in Pichia pastoris
expression in Pichia pastoris; expression in Pichia pastoris
expression in protease-free Thielavia heterothallica
-
expression in Trichoderma reesei
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
Y116F
no changes in the C1:C4 oxidation ratio
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
-
Y116F
-
no changes in the C1:C4 oxidation ratio
-
A143C/P183C/S73C/A115C
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
S73C/A115C
-
introduction of an additional disulfide bridge, mutant displays a 9°C increase in melting temperature
W88Y/N91F
-
mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54
A143C/P183C/S73C/A115C
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introduction of addtitional disulfide bridges A143C-P183C and S73C-A115C, increase in melting temperature by 12 degrees; introduction of two additional disulfide bridges, mutant displays a 12°C increase in melting temperature and is able to retain 60% of its activity after heat treatment
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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
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S73C/A115C
-
introduction of an additional disulfide bridge, mutant displays a 9°C increase in melting temperature
-
W88Y/N91F
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mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
degradation
synthesis