Information on EC 1.14.99.B6 - lytic cellulose monooxygenase (C1-hydroxylating)

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.14.99.B6
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
lytic cellulose monooxygenase (C1-hydroxylating)
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
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
SYSTEMATIC NAME
IUBMB Comments
cellulose, hydrogen-donor:oxygen oxidoreductase (D-glucosyl C1-hydroxylating)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Thielavia heterothallica
UniProt
Manually annotated by BRENDA team
Thielavia heterothallica
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
mangrove-associated fungus
KR825269, KR825270
Genbank
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
microcrystalline cellulose + AH2 + O2
?
show the reaction diagram
-
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
show the reaction diagram
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
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
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
-
?
xyloglucan + ascorbate + O2
?
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
?
-
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
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cellobiose dehydrogenase
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8
assay at; assay at
5.5
KR825269, KR825270
;
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6.5
KR825269, KR825270
no activity below pH 4.5; no activity below pH 4.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
assay at; assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22770
mass spectrometry
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methylation
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
60
KR825269, KR825270
considerably stable; fast degradation
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nickel chelate His-bind resin column chomatography; nickel chelate His-bind resin column chomatography
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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