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Enzyme Nomenclature
Information on EC 1.14.99.53 - lytic chitin monooxygenase
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1.14.99.53 lytic chitin monooxygenaseIUBMB Comments
The enzyme cleaves chitin in an oxidative manner, releasing fragments of chitin with an N-acetylamino-D-glucono-1,5-lactone at the reducing end. The initially formed lactone at the reducing end of the shortened chitin chain quickly hydrolyses spontaneously to the aldonic acid. In vitro ascorbate can serve as reducing agent. The enzyme contains copper at the active site.
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Word Map
- 1.14.99.53
- polysaccharide
- chitinases
-
lpmos
-
recalcitrant
-
chitinolytic
- cellulose
- biomass
-
c1-oxidizer
- analysis
- synthesis
-
listeria
- transposon
- monocytogenes
- degradation
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AA10
AO090102000501
BATR1942_08650
BURPS1710b_0114
CelS2
EF_0362
GbpA
-
virulence factor with no obvious role in biomass processing
Jden_1381
lmo2467
LPMO10
LPMO10A
LPMO10B
LPMO10F
Micau_1630
RBAM17540
SCO0643
SGR_6855
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[(1->4)-N-acetyl-beta-D-glucosaminyl](m+n) + reduced acceptor + O2 = [(1->4)-N-acetyl-beta-D-glucosaminyl](m-1)-(1->4)-2-(acetylamino)-2-deoxy-D-glucono-1,5-lactone + [(1->4)-N-acetyl-beta-D-glucosaminyl]n + acceptor + H2O
[(1->4)-N-acetyl-beta-D-glucosaminyl](m+n) + reduced acceptor + O2 = [(1->4)-N-acetyl-beta-D-glucosaminyl](m-1)-(1->4)-2-(acetylamino)-2-deoxy-D-glucono-1,5-lactone + [(1->4)-N-acetyl-beta-D-glucosaminyl]n + acceptor + H2O
(1) the initially formed D-glucono-1,5-lactone at the reducing end of the chitin chain quickly hydrolyzes spontaneously to the aldonic acid
[(1->4)-N-acetyl-beta-D-glucosaminyl](m+n) + reduced acceptor + O2 = [(1->4)-N-acetyl-beta-D-glucosaminyl](m-1)-(1->4)-2-(acetylamino)-2-deoxy-D-glucono-1,5-lactone + [(1->4)-N-acetyl-beta-D-glucosaminyl]n + acceptor + H2O
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
,
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SYSTEMATIC NAME
IUBMB Comments
chitin, hydrogen-donor:oxygen oxidoreductase (N-acetyl-beta-D-glucosaminyl C1-hydroxylating/C4-dehdrogenating)
The enzyme cleaves chitin in an oxidative manner, releasing fragments of chitin with an N-acetylamino-D-glucono-1,5-lactone at the reducing end. The initially formed lactone at the reducing end of the shortened chitin chain quickly hydrolyses spontaneously to the aldonic acid. In vitro ascorbate can serve as reducing agent. The enzyme contains copper at the active site.
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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
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
-
-
-
?
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 + ascorbic acid + O2
? + dehydroascorbate + H2O
-
-
-
-
?
beta-chitin + cellobiose dehydrogenase + O2
C1-oxidized oligosaccharides + reduced cellobiose dehydrogenase + H2O
chitin + acceptor + O2
[chitin oligosaccharide]-N-acetyl-D-glucosaminate + [chitin oligosaccharide]-N-acetyl-D-glucosamino-1,5-lactone
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
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
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
Cu2+
additional information
residues His28 and His114 in the catalytic center bind a variety of divalent metal ions such as Ca2+, Mg2+, Fe3+, Co2+, Zn2+, or Cu2+ with a clear preference for Cu2+
copper
a putative dioxygen species is equatorially bound to the active site copper, consistent with a Cu(II)-bound peroxide. The coordination environment is consistent with Cu(II)
Cu2+
-
Cu(II) binds with KD value 43 nM at pH 5. The coordination geometry around the copper is distorted from axial symmetry
Cu2+
the active site contains a copper ion coordinated by residues His-37 and His-136 in a T-shaped histidine brace
Cu2+
structural changes observed upon irradiation of CBM33A reflect photoreduction of Cu(II) to Cu(I). Charges found in the formal Cu(II) and Cu(I) oxidation states are 1.48 and 0.92, respectively
Cu2+
crystal structures show a putative dioxygen species equatorially bound to the active site copper
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+
Kd value 55 nM, from isothermal titration calorimetry, and for Cu1+, Kd value 1 nM from the experimentally determined redox potential
Cu2+
the copper site is highly similar to that of the C1/C4 cellulose-oxidizing LPMO9A from Thermoascus aurantiacus and exhibits an octahedral coordination geometry with Jahn-Teller distortion. Dissociation constant is 12 nM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Expression of chitinases in Listeria monocytogenes is influenced by lmo0327 that encodes an internalin-like protein.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
protein comprises a small N-terminal LPMO10 module named LPMO10A followed by a family 5/12 CBM and a C-terminal GH18 module
UniProt
brenda
protein comprises a small N-terminal LPMO10 module named LPMO10A followed by a family 5/12 CBM and a C-terminal GH18 module
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
cellobiose dehydrogenase from Myriococcum thermophilum can act as an electron donor. Employing the enzyme as electron donor enables a kinetically controlled supply of electrons to the LPMO. The rate of chitin oxidation by CBP21 is equal to that of cosubstrate (lactose) oxidation by cellobiose dehydrogenase, verifying the usage of two electrons in the LPMO catalytic mechanism. Lactose oxidation correlates directly with the rate of LPMO catalysis, a method for indirect determination of LPMO activity is implicated
physiological function
enzyme increases chitin solubilization yields of chitinases by up to 30fold and 20fold for alpha- and beta-chitin, respectively. The addition of LPMO10F leads to a substantial increase in the (GlcNAc)2:GlcNAc product ratio of chitinases, in reactions with alpha-chitin only
physiological function
in presence of lytic polysaccharide monooxygenase Cbp21, the apparent kcat values of chitinases ChiA and ChiB increase 6-9fold, while there is no effect on chitinase ChiC
physiological function
LPMO10 and a chitinase mutually enhance each others activities upon degrading chitin as the substrate
phys