HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 1.14.99.B6 - lytic cellulose monooxygenase (C1-hydroxylating)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.14.99.B6
preliminary BRENDA-supplied EC number
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
lytic cellulose monooxygenase (C1-hydroxylating)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[(1->4)-beta-D-glucosyl]n+m + AH2 + O2 = 4-dehydro-beta-D-glucosyl-[(1->4)-beta-D-glucosyl]n-1 + [(1->4)-beta-D-glucosyl]m + A + H2O
[(1->4)-beta-D-glucosyl]n+m + AH2 + O2 = [(1->4)-beta-D-glucosyl]m-1-(1->4)-D-glucono-1,5-lactone + [(1->4)-beta-D-glucosyl]n + A + H2O
[(1->4)-beta-D-glucosyl]n+m + AH2 + O2 = 4-dehydro-beta-D-glucosyl-[(1->4)-beta-D-glucosyl]n-1 + [(1->4)-beta-D-glucosyl]m + A + H2O
(2) the enzyme cleaves cellulose in an oxidative manner in two ways and releases cellulose fragments with an aldonic acid at the reducing end as well as cellulose fragments with a 4-dehydro-D-glucose residue at the non-reducing end. Ascorbate has been found to be able to act as reducing agent.
[(1->4)-beta-D-glucosyl]n+m + AH2 + O2 = 4-dehydro-beta-D-glucosyl-[(1->4)-beta-D-glucosyl]n-1 + [(1->4)-beta-D-glucosyl]m + A + H2O
(2) the enzyme cleaves cellulose in an oxidative manner in two ways and releases cellulose fragments with an aldonic acid at the reducing end as well as cellulose fragments with a 4-dehydro-D-glucose residue at the non-reducing end. Ascorbate has been found to be able to act as reducing agent.
-
-
[(1->4)-beta-D-glucosyl]n+m + AH2 + O2 = 4-dehydro-beta-D-glucosyl-[(1->4)-beta-D-glucosyl]n-1 + [(1->4)-beta-D-glucosyl]m + A + H2O
-
-
-
-
[(1->4)-beta-D-glucosyl]n+m + AH2 + O2 = [(1->4)-beta-D-glucosyl]m-1-(1->4)-D-glucono-1,5-lactone + [(1->4)-beta-D-glucosyl]n + A + H2O
(1) the D-glucono-1,5-lactone at the reducing end of the cellulose chain quickly hydrolyzes spontaneuosly to the aldonic acid
[(1->4)-beta-D-glucosyl]n+m + AH2 + O2 = [(1->4)-beta-D-glucosyl]m-1-(1->4)-D-glucono-1,5-lactone + [(1->4)-beta-D-glucosyl]n + A + H2O
(1) the D-glucono-1,5-lactone at the reducing end of the cellulose chain quickly hydrolyzes spontaneuosly to the aldonic acid
-
-
[(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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
cellulose, hydrogen-donor:oxygen oxidoreductase (D-glucosyl C1-hydroxylating)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme has both C1-hydroxylating and C4-dehydrogenating activities
UniProt
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
amorphous cellulose + 2 AH2 + 2 O2
cellooligosaccharide-C6-aldehyde-C1-lactone + 2 A + 2 H2O
microcrystalline cellulose + AH2 + O2
?
-
enzyme catalyzes release of a mixture of soluble sugars comprising reduced and oxidized cellooligosaccharides. The degree of polymerization of the released oligosaccharides ranges from 3 to 5 for the reduced products and from 2 to 5 for the oxidized products
-
?
phosphoric acid swollen cellulose + ascorbate + O2
C4-dehydro-cellooligosaccharide + dehydroascorbate + 2 H2O
KR825269, KR825270
-
The chain lengths of the cellooligosaccharides ranges from 2 to 5
-
?
phosphoric acid swollen cellulose + ascorbate + O2
C4-dehydro-cellooligosaccharide-C1-lactone + dehydroascorbate + H2O
KR825269, KR825270
-
the initially formed lactone at the reducing end of the produced cellooligosaccharides is hydrolyzed spontanously to the aldonic acid. The chain lengths of the cellooligosaccharides ranges from 2 to 5
-
?
phosphoric acid swollen cellulose + ascorbate + O2
cellooligosaccharide-C1-lactone + dehydroascorbate + H2O
KR825269, KR825270
-
the initially formed lactone at the reducing end of the produced cellooligosaccharides is hydrolyzed spontanously to the aldonic acid. The chain lengths of the cellooligosaccharides ranges from 2 to 5
-
?
[(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
amorphous cellulose + 2 AH2 + 2 O2
cellooligosaccharide-C6-aldehyde-C1-lactone + 2 A + 2 H2O
-
the initially formed lactone at the reducing end of the produced cellooligosaccharides is hydrolyzed spontanously to the aldonic acid. The chain lengths of the cellooligosaccharides ranges from 2 to 5
-
?
amorphous cellulose + 2 AH2 + 2 O2
cellooligosaccharide-C6-aldehyde-C1-lactone + 2 A + 2 H2O
-
the initially formed lactone at the reducing end of the produced cellooligosaccharides is hydrolyzed spontanously to the aldonic acid. The chain lengths of the cellooligosaccharides ranges from 2 to 5
-
?
amorphous cellulose + AH2 + O2
cellooligosaccharide-C1-lactone + A + H2O
-
the initially formed lactone at the reducing end of the produced cellooligosaccharides is hydrolyzed spontanously to the aldonic acid. The chain lengths of the cellooligosaccahdides ranges from 2 to 5
-
?
amorphous cellulose + AH2 + O2
cellooligosaccharide-C1-lactone + A + H2O
-
the initially formed lactone at the reducing end of the produced cellooligosaccharides is hydrolyzed spontanously to the aldonic acid. The chain lengths of the cellooligosaccharides ranges from 2 to 5
-
?
amorphous cellulose + AH2 + O2
cellooligosaccharide-C1-lactone + A + H2O
-
the initially formed lactone at the reducing end of the produced cellooligosaccharides is hydrolyzed spontanously to the aldonic acid. The chain lengths of the cellooligosaccahdides ranges from 2 to 5
-
?
amorphous cellulose + AH2 + O2
cellooligosaccharide-C1-lactone + A + H2O
-
the initially formed lactone at the reducing end of the produced cellooligosaccharides is hydrolyzed spontanously to the aldonic acid. The chain lengths of the cellooligosaccharides ranges from 2 to 5
-
?
[(1->4)-beta-D-glucosyl]n+m + AH2 + O2
[(1->4)-beta-D-glucosyl]m-1-(1->4)-D-glucono-1,5-lactone + [(1->4)-beta-D-glucosyl]n + A + H2O
-
-
-
?
[(1->4)-beta-D-glucosyl]n+m + AH2 + O2
[(1->4)-beta-D-glucosyl]m-1-(1->4)-D-glucono-1,5-lactone + [(1->4)-beta-D-glucosyl]n + A + H2O
-
-
-
?
[(1->4)-beta-D-xylosyl]6-(1->4)-beta-D-glucose + ascorbate + O2
?
-
-
-
-
[(1->4)-beta-D-xylosyl]6-(1->4)-beta-D-glucose + ascorbate + O2
?
-
-
-
-
additional information
?
-
The enzyme also oxidizes wheat arabinoxylan, birchwood glucuronoxylan and oat spelt xylan if assayed in the presence of amorphous cellulose. The enzyme uses cellulose to bind while oxidizing neighboring xylan chains. No activity is observed with wheat arabinoxylan, birchwood glucuronoxylan and oat spelt xylan alone
-
-
-
additional information
?
-
The enzyme also oxidizes wheat arabinoxylan, birchwood glucuronoxylan and oat spelt xylan if assayed in the presence of amorphous cellulose. The enzyme uses cellulose to bind while oxidizing neighboring xylan chains. No activity is observed with wheat arabinoxylan, birchwood glucuronoxylan and oat spelt xylan alone
-
-
-
additional information
?
-
-
The enzyme also oxidizes wheat arabinoxylan, birchwood glucuronoxylan and oat spelt xylan if assayed in the presence of amorphous cellulose. The enzyme uses cellulose to bind while oxidizing neighboring xylan chains. No activity is observed with wheat arabinoxylan, birchwood glucuronoxylan and oat spelt xylan alone
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
[(1->4)-beta-D-glucosyl]n+m + AH2 + O2
[(1->4)-beta-D-glucosyl]m-1-(1->4)-D-glucono-1,5-lactone + [(1->4)-beta-D-glucosyl]n + A + H2O
[(1->4)-beta-D-glucosyl]n+m + AH2 + O2
[(1->4)-beta-D-glucosyl]m-1-(1->4)-D-glucono-1,5-lactone + [(1->4)-beta-D-glucosyl]n + A + H2O
A0A0H4K9X4
-
-
-
?
[(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
A0A0H4K9X4
-
-
-
?
additional information
?
-
A0A0H4K9X4
The enzyme also oxidizes wheat arabinoxylan, birchwood glucuronoxylan and oat spelt xylan if assayed in the presence of amorphous cellulose. The enzyme uses cellulose to bind while oxidizing neighboring xylan chains. No activity is observed with wheat arabinoxylan, birchwood glucuronoxylan and oat spelt xylan alone
-
-
-
additional information
?
-
A0A0H4K9X4
The enzyme also oxidizes wheat arabinoxylan, birchwood glucuronoxylan and oat spelt xylan if assayed in the presence of amorphous cellulose. The enzyme uses cellulose to bind while oxidizing neighboring xylan chains. No activity is observed with wheat arabinoxylan, birchwood glucuronoxylan and oat spelt xylan alone
-
-
-
additional information
?
-
-
The enzyme also oxidizes wheat arabinoxylan, birchwood glucuronoxylan and oat spelt xylan if assayed in the presence of amorphous cellulose. The enzyme uses cellulose to bind while oxidizing neighboring xylan chains. No activity is observed with wheat arabinoxylan, birchwood glucuronoxylan and oat spelt xylan alone
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
Cu2+
The copper ion lies in the center of a flat surface that interacts with the substrate. The equatorial plane includes the protein's N-terminal Ndelta of His-1 and the Nepsilon of His-83
Cu2+
KR825269, KR825270
strictly conserved copper-binding site which consists of two histidines (one at N-terminal position) and one tyrosine; strictly conserved copper-binding site which consists of two histidines (one at N-terminal position) and one tyrosine
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cellobiose dehydrogenase
KR825269, KR825270
physiological electron donor; physiological electron donor
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6.5
KR825269, KR825270
no activity below pH 4.5; no activity below pH 4.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methylation
methylation
the enzyme contains an N-methylated histidine at the N-terminus
methylation
-
the enzyme contains an N-methylated histidine at the N-terminus
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nickel chelate His-bind resin column chomatography; nickel chelate His-bind resin column chomatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
expressed in Pichia pastoris; expressed in Pichia pastoris
KR825269, KR825270
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
design of dockerin-fused lytic polysaccharide monooxygenases. The resulting chimeras exhibit activity levels on microcrystalline cellulose similar to that of the wild-type enzymes. The dockerin moieties of the chimeras are functional and specifically bind to their corresponding cohesin partner. The chimeric lytic polysaccharide monooxygenases are able to self-assemble in designer cellulosomes alongside an endo- and an exo-cellulase also converted to the cellulosomal mode. The resulting complexes show a 1.7fold increase in the release of soluble sugars from cellulose, compared with the free enzymes, and a 2.6fold enhancement compared with free cellulases without lytic polysaccharide monooxygenase enhancement; design of dockerin-fused lytic polysaccharide monooxygenases. The resulting chimeras exhibit activity levels on microcrystalline cellulose similar to that of the wild-type enzymes. The dockerin moieties of the chimeras are functional and specifically bind to their corresponding cohesin partner. The chimeric lytic polysaccharide monooxygenases are able to self-assemble in designer cellulosomes alongside an endo- and an exo-cellulase also converted to the cellulosomal mode. The resulting complexes show a 1.7fold increase in the release of soluble sugars from cellulose, compared with the free enzymes, and a 2.6fold enhancement compared with free cellulases without lytic polysaccharide monooxygenase enhancement
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 1.14.99.B6)
html completed
Information
