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Information on EC 1.14.99.53 - lytic chitin monooxygenase
for references in articles please use BRENDA:EC1.14.99.53
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.99 Miscellaneous
1.14.99.53 lytic chitin monooxygenase
IUBMB 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.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 1.14.99.53
- polysaccharide
- chitinases
-
lpmos
-
recalcitrant
-
chitinolytic
- cellulose
- biomass
-
c1-oxidizer
- analysis
- synthesis
-
listeria
- transposon
- monocytogenes
- degradation
Reaction Schemes
showSynonyms
lpmo10, lmo2467, lytic chitin monooxygenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AA10
AA10A
AA11
AO090102000501
BATR1942_08650
BURPS1710b_0114
CbpD
CCT67099
CelS2
chitin-binding domain 3 protein
EF_0362
GbpA
Jden_1381
lmo2467
LPMO10
LPMO10A
LPMO10B
LPMO10F
Micau_1630
RBAM17540
SCO0643
SGR_199
SGR_6855
GbpA
-
virulence factor with no obvious role in biomass processing
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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
MetaCyc
chitin degradation II (Vibrio), chitin degradation III (Serratia)
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-chitin + ascorbate + O2
chito-oligosaccharide aldonic acid + dehydroascorbate + H2O
Substrates: -
Products: products show a degree of polymerization from DP3 to DP8, with DP6 being the most abundant product after 24 h of incubation
Products: 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
Substrates: -
Products: -
Products: -
?
alpha-chitin + gallate + O2
chito-oligosaccharide + C1-aldonic acids + ? + H2O
-
Substrates: -
Products: -
Products: -
?
alpha-chitin + gallate + O2
chito-oligosaccharide C1-aldonic acids + dehydroascorbate + H2O
beta-chitin + acceptor + O2
chito-oligosaccharide aldonic acid + reduced acceptor + H2O
Substrates: -
Products: products show a degree of polymerization from DP3 to DP8, with DP6 being the most abundant product after 24 h of incubation
Products: 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
-
Substrates: -
Products: -
Products: -
?
beta-chitin + cellobiose dehydrogenase + O2
C1-oxidized oligosaccharides + reduced cellobiose dehydrogenase + H2O
cellulose + ascorbate + O2
? + dehydroascorbate + H2O
-
Substrates: -
Products: -
Products: -
?
chitin + acceptor + O2
? + reduced acceptor + H2O
Substrates: -
Products: -
Products: -
?
chitin + acceptor + O2
[chitin oligosaccharide]-N-acetyl-D-glucosaminate + [chitin oligosaccharide]-N-acetyl-D-glucosamino-1,5-lactone
chitin + ascorbate + O2
C1-oxidized chito-oligosaccharides + dehydroascorbate + H2O
-
Substrates: -
Products: -
Products: -
?
chitin + ascorbate + O2
chito-oligosaccharide + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
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
[(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
Substrates: -
Products: -
Products: -
?
[(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
-
Substrates: -
Products: -
Products: -
?
alpha-chitin + acceptor + O2
oligosaccharide aldonic acids + reduced acceptor + H2O
-
Substrates: -
Products: -
Products: -
?
alpha-chitin + acceptor + O2
oligosaccharide aldonic acids + reduced acceptor + H2O
Substrates: -
Products: -
Products: -
?
alpha-chitin + acceptor + O2
oligosaccharide aldonic acids + reduced acceptor + H2O
Fusarium fujikuroi CBS 195.34
Substrates: -
Products: -
Products: -
?
alpha-chitin + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: products are the aldonic acid forms of fully acetylated chitooligosaccharides, oxidation occurs at the C1 carbon atom
Products: products are the aldonic acid forms of fully acetylated chitooligosaccharides, oxidation occurs at the C1 carbon atom
?
alpha-chitin + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: products are the aldonic acid forms of fully acetylated chitooligosaccharides, oxidation occurs at the C1 carbon atom
Products: products are the aldonic acid forms of fully acetylated chitooligosaccharides, oxidation occurs at the C1 carbon atom
?
alpha-chitin + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
alpha-chitin + ascorbate + O2
? + dehydroascorbate + H2O
Trichoderma guizhouense NJAU 47420
Substrates: -
Products: -
Products: -
?
alpha-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: products are C1-oxidized chitooligomers, mainly tetramers and hexamers
Products: products are C1-oxidized chitooligomers, mainly tetramers and hexamers
?
alpha-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: products are C1-oxidized chitooligomers, mainly tetramers and hexamers
Products: products are C1-oxidized chitooligomers, mainly tetramers and hexamers
?
alpha-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
Substrates: enzyme shows stronger binding and a greater release of soluble oxidized products with beta-chitin than with alpha-chitin
Products: products show oxidation of the C1 carbon leading to aldonic acids
Products: products show oxidation of the C1 carbon leading to aldonic acids
?
alpha-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
Substrates: enzyme shows stronger binding and a greater release of soluble oxidized products with beta-chitin than with alpha-chitin
Products: products show oxidation of the C1 carbon leading to aldonic acids
Products: products show oxidation of the C1 carbon leading to aldonic acids
?
alpha-chitin + ascorbate + O2
oxidized oligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
alpha-chitin + ascorbate + O2
oxidized oligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
alpha-chitin + gallate + O2
? + H2O
Substrates: -
Products: -
Products: -
?
alpha-chitin + gallate + O2
chito-oligosaccharide C1-aldonic acids + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
alpha-chitin + gallate + O2
chito-oligosaccharide C1-aldonic acids + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
beta-chitin + acceptor + O2
chito-oligosaccharide aldonic acids + reduced acceptor + H2O
Substrates: -
Products: -
Products: -
?
beta-chitin + acceptor + O2
chito-oligosaccharide aldonic acids + reduced acceptor + H2O
Substrates: -
Products: -
Products: -
?
beta-chitin + acceptor + O2
oligosaccharide aldonic acids + reduced acceptor + H2O
-
Substrates: beta chitin from squid pen, best substrate
Products: strong preference towards even-numbered products
Products: strong preference towards even-numbered products
?
beta-chitin + acceptor + O2
oligosaccharide aldonic acids + reduced acceptor + H2O
-
Substrates: beta chitin from squid pen, best substrate
Products: strong preference towards even-numbered products
Products: strong preference towards even-numbered products
?
beta-chitin + acceptor + O2
oligosaccharide aldonic acids + reduced acceptor + H2O
Substrates: -
Products: -
Products: -
?
beta-chitin + acceptor + O2
oligosaccharide aldonic acids + reduced acceptor + H2O
Fusarium fujikuroi CBS 195.34
Substrates: -
Products: -
Products: -
?
beta-chitin + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
beta-chitin + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
beta-chitin + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: products are the aldonic acid forms of fully acetylated chitooligosaccharides, oxidation occurs at the C1 carbon atom
Products: products are the aldonic acid forms of fully acetylated chitooligosaccharides, oxidation occurs at the C1 carbon atom
?
beta-chitin + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: products are the aldonic acid forms of fully acetylated chitooligosaccharides, oxidation occurs at the C1 carbon atom
Products: products are the aldonic acid forms of fully acetylated chitooligosaccharides, oxidation occurs at the C1 carbon atom
?
beta-chitin + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
beta-chitin + ascorbate + O2
? + dehydroascorbate + H2O
Trichoderma guizhouense NJAU 47420
Substrates: -
Products: -
Products: -
?
beta-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
Substrates: beta-chitin is preferred over alpha-chitin
Products: products are C1-oxidized chitooligomers, mainly tetramers and hexamers
Products: products are C1-oxidized chitooligomers, mainly tetramers and hexamers
?
beta-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
Substrates: beta-chitin is preferred over alpha-chitin
Products: products are C1-oxidized chitooligomers, mainly tetramers and hexamers
Products: products are C1-oxidized chitooligomers, mainly tetramers and hexamers
?
beta-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
beta-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
Substrates: enzyme shows stronger binding and a greater release of soluble oxidized products with beta-chitin than with alpha-chitin
Products: products show oxidation of the C1 carbon leading mainly to tetrameric and hexameric aldonic acids
Products: products show oxidation of the C1 carbon leading mainly to tetrameric and hexameric aldonic acids
?
beta-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
Substrates: enzyme shows stronger binding and a greater release of soluble oxidized products with beta-chitin than with alpha-chitin
Products: products show oxidation of the C1 carbon leading mainly to tetrameric and hexameric aldonic acids
Products: products show oxidation of the C1 carbon leading mainly to tetrameric and hexameric aldonic acids
?
beta-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
-
Substrates: -
Products: -
Products: -
?
beta-chitin + ascorbate + O2
C1-oxidized oligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
beta-chitin + ascorbate + O2
C1-oxidized oligosaccharides + dehydroascorbate + H2O
Substrates: substrate squid pen beta-chitin
Products: in addition, considerable amounts of partially deacetylated oligomers are produced
Products: in addition, considerable amounts of partially deacetylated oligomers are produced
?
beta-chitin + ascorbate + O2
C1-oxidized oligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
beta-chitin + ascorbate + O2
C1-oxidized oligosaccharides + dehydroascorbate + H2O
Substrates: substrate squid pen beta-chitin
Products: in addition, considerable amounts of partially deacetylated oligomers are produced
Products: in addition, considerable amounts of partially deacetylated oligomers are produced
?
beta-chitin + ascorbate + O2
oxidized oligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
beta-chitin + ascorbate + O2
oxidized oligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
beta-chitin + cellobiose dehydrogenase + O2
C1-oxidized oligosaccharides + reduced cellobiose dehydrogenase + H2O
Substrates: cellobiose dehydrogenase from Myriococcum thermophilum can act as an electron donor
Products: -
Products: -
?
beta-chitin + cellobiose dehydrogenase + O2
C1-oxidized oligosaccharides + reduced cellobiose dehydrogenase + H2O
Substrates: cellobiose dehydrogenase from Myriococcum thermophilum can act as an electron donor
Products: -
Products: -
?
chitin + acceptor + O2
C1-oxidized chito-oligosaccharides + reduced acceptor + H2O
Substrates: -
Products: 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
Products: 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
Substrates: -
Products: 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
Products: 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
Substrates: -
Products: 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.
Products: 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
Substrates: -
Products: 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.
Products: 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
D9SZQ3
Substrates: -
Products: -
Products: -
?
chitin + ascorbic acid + O2
? + dehydroascorbate + H2O
Micromonospora aurantiaca (nom. illeg.) DSM 43813
D9SZQ3
Substrates: -
Products: -
Products: -
?
chitin + ascorbic acid + O2
? + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
chitin + ascorbic acid + O2
? + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
colloidal chitin + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: low activity, products show less dominance of even-numbered products than alpha- or beta-chitin
Products: low activity, products show less dominance of even-numbered products than alpha- or beta-chitin
?
colloidal chitin + ascorbate + O2
? + dehydroascorbate + H2O
Substrates: -
Products: low activity, products show less dominance of even-numbered products than alpha- or beta-chitin
Products: low activity, products show less dominance of even-numbered products than alpha- or beta-chitin
?
colloidal chitin + ascorbate + O2
oxidized chitin oligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: with colloidal chitin as the substrate, a ladder of oxidized oligosaccharides is observed
Products: with colloidal chitin as the substrate, a ladder of oxidized oligosaccharides is observed
?
colloidal chitin + ascorbate + O2
oxidized chitin oligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: with colloidal chitin as the substrate, a ladder of oxidized oligosaccharides is observed
Products: 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
A0A0H3E2X6
Substrates: -
Products: -
Products: -
?
colloidal chitin + ascorbate + O2
[chitin oligosaccharide]-N-acetyl-D-glucosaminate + [chitin oligosaccharide]-N-acetyl-D-glucosamino-1,5-lactone + dehydroascorbate + H2O
A0A0H3E2X6
Substrates: -
Products: -
Products: -
?
crystalline chitin + ascorbate + O2
oxidized oligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: enzyme generates even-numbered oxidized oligosaccharides as the dominated products from crystalline chitin
Products: enzyme generates even-numbered oxidized oligosaccharides as the dominated products from crystalline chitin
?
crystalline chitin + ascorbate + O2
oxidized oligosaccharides + dehydroascorbate + H2O
Substrates: -
Products: enzyme generates even-numbered oxidized oligosaccharides as the dominated products from crystalline chitin
Products: enzyme generates even-numbered oxidized oligosaccharides as the dominated products from crystalline chitin
?
phosphoric acid swollen cellulase + ascorbic acid + O2
? + dehydroascorbate + H2O
D9SZQ3
Substrates: -
Products: -
Products: -
?
phosphoric acid swollen cellulase + ascorbic acid + O2
? + dehydroascorbate + H2O
Micromonospora aurantiaca (nom. illeg.) DSM 43813
D9SZQ3
Substrates: -
Products: -
Products: -
?
phosphoric acid swollen cellulase + ascorbic acid + O2
? + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
phosphoric acid swollen cellulase + ascorbic acid + O2
? + dehydroascorbate + H2O
Substrates: -
Products: -
Products: -
?
phosphoric acid swollen cellulose + ascorbate + O2
C4-oxidized cellooligosaccharides + C1/C4-oxidized cellooligosaccharides + dehydroascorbate + H2O
Substrates: reaction of EC 1.14.99.54
Products: -
Products: -
?
phosphoric acid swollen cellulose + ascorbate + O2
C4-oxidized cellooligosaccharides + C1/C4-oxidized cellooligosaccharides + dehydroascorbate + H2O
Substrates: reaction of EC 1.14.99.54
Products: -
Products: -
?
[(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
Substrates: -
Products: -
Products: -
?
[(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
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: presence of ascorbate is required. No substrates: phosphoric acid-swollen cellulose, avicel, tamarind xyloglucan, birchwood xylan, beechwood xylan, acetyl glucuronoxylan from aspen, ivory nut mannan, acetylated konjac glucomannan, potato starch, heparin, hyaluronic acid, and chitosan
Products: -
Products: -
?
additional information
?
-
Substrates: presence of ascorbate is required. No substrates: phosphoric acid-swollen cellulose, avicel, tamarind xyloglucan, birchwood xylan, beechwood xylan, acetyl glucuronoxylan from aspen, ivory nut mannan, acetylated konjac glucomannan, potato starch, heparin, hyaluronic acid, and chitosan
Products: -
Products: -
?
additional information
?
-
Substrates: no activity on other substrates including diverse mannans, cellulose and starch
Products: -
Products: -
?
additional information
?
-
Substrates: no activity on other substrates including diverse mannans, cellulose and starch
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: data indicate that catalysis involves equatorial binding of a reactive oxygen species
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is active on alpha- and beta-chitin, and the chitin-binding surface previously described for larger LPMOs is fully conserved
Products: -
Products: -
?
additional information
?
-
Substrates: data indicate that catalysis involves equatorial binding of a reactive oxygen species
Products: -
Products: -
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additional information
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Substrates: the enzyme is active on alpha- and beta-chitin, and the chitin-binding surface previously described for larger LPMOs is fully conserved
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additional information
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Substrates: enzyme binds to cellulose, but does not display catalyic activity
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additional information
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Substrates: enzyme binds to cellulose, but does not display catalyic activity
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additional information
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Substrates: 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
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Substrates: [(1->4)-N-acetyl-beta-D-glucosaminyl]6 is a substrate, but not shorter oligomers
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additional information
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Substrates: enzyme additionally shows peroxigenase activity. The peroxygenase reaction is faster than the monooxygenase reaction
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additional information
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Substrates: enzyme in presence of ascorbate but lacking chitin produces H2O2
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additional information
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Substrates: isoform LPMO10B produces C4-oxidized (4-ketoaldoses) and double (C4/C1)-oxidized cello-oligosaccharides. No substrate: alpha-chitin
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additional information
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Substrates: enzyme additionally shows peroxigenase activity. The peroxygenase reaction is faster than the monooxygenase reaction
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additional information
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Substrates: enzyme in presence of ascorbate but lacking chitin produces H2O2
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additional information
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Substrates: isoform LPMO10B produces C4-oxidized (4-ketoaldoses) and double (C4/C1)-oxidized cello-oligosaccharides. No substrate: alpha-chitin
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
Cu2+
additional information
copper
D9SZQ3
the active site is formed by His37 and His144 that coordinate the copper atom in a T-shaped geometry
copper
Cu2+ does not dissociate from the protein molecule during unfolding
copper
tight binding activity toward Cu2+ , Kd value 0.0048 mM. Residues His1 and His61 directly coordinate the basic copper cofactor in T-shaped geometry
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+
D9SZQ3
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
additional information
-
enzyme is highly tolerant and stable in presence of up to 1 M metal ions
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+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
azurin
1 microM azurin activates 1 microM copper-free CbpD, which otherwise is inactive
H2O2
catalytic activity of AA11A on chitin increases in presence of H2O2
pyocyanin
boosts CbpD activity towards beta-chitin, with rapid inactivation abocve 1 M
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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
Micromonospora aurantiaca (nom. illeg.) DSM 43813
cf. EC 1.14.99.56, 1.14.99.54
D9SZQ3
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
AaAA15A is the most highly expressed AA15-encoding gene in both sporulating and growing mycelia
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
enzyme has two carbohydrate-binding modules, CBM5 and CBM73. Both CBMs bind crystalline chitin with Kd values in the micromolar range, CBM73 has higher affinity for chitin than CjCBM5. CBM5 binds soluble chitohexaose, whereas no binding of CBM73 chitohexaose is detected. In CBM5, conserved aromatic amino acids involved in substrate binding residues show a linear arrangement that seems compatible with the experimentally observed affinity for single chitin chains. The arrangement of these residues in CBM73 suggests a wider binding surface that may interact with several chitin chains
metabolism
-
role of LPMO's structural dynamics during polysaccharide degradation, comparison of multiple LPMO structures. The substrate binding region is highly flexible with significant and sustained micro-scale level conformational changes.The loops on the binding side of the substrate are most mobile, in concert with the dynamic modes influencing the motions during binding. There are dynamic differences between families AA9, AA10, AA11, and AA13 that consist of more than one structure. The patterns of motion in the loop regions among the AA9 structures are distinct from those in the AA10 structures
metabolism
-
enzyme has two carbohydrate-binding modules, CBM5 and CBM73. Both CBMs bind crystalline chitin with Kd values in the micromolar range, CBM73 has higher affinity for chitin than CjCBM5. CBM5 binds soluble chitohexaose, whereas no binding of CBM73 chitohexaose is detected. In CBM5, conserved aromatic amino acids involved in substrate binding residues show a linear arrangement that seems compatible with the experimentally observed affinity for single chitin chains. The arrangement of these residues in CBM73 suggests a wider binding surface that may interact with several chitin chains
-
physiological function
presence of CBP21 increases solubilization of chitin substrates with high degrees of crystallinity when combined with each of the three chitinases ChiA, ChiB, or ChiC, but this synergy is reduced upon decline in crystallinity
physiological function
the full-length enzyme and the individual catalytic LPMO module boost the activity of an endochitinase equally well, also yielding similar amounts of oxidized products. When grown on insoluble chitin substrates, the deletion mutant shows a reproducible growth defect on beta-chitin leading to an 2fold slower growth rate compared with the wild type strain. When grown on crab shells, the mutation leads to an extended lag phase of about 100 h
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
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
A0A0H3E2X6
LPMO10 and a chitinase mutually enhance each others activities upon degrading chitin as the substrate
physiological function
presence of LPMO10 increases the rate of chitin depolymerization by both chitinases ChiA and ChiB
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
-
downregulation of LPMO15-3 expression at the 4th or 5th instar nymph stage severely decreases the survival rate and results in lethal phenotypes. The deficient individuals exhibit incompletely digested peritrophic matrix
physiological function
member of lytic polysaccharide monooxygenase family AA11
physiological function
enzyme produces oxidized cello-oligosaccharides from cellulose and boosts cellulose degradation by cellulases. The binding ability of LPMO10A depends on carbohydrate binding module CBM2
physiological function
deletion of cbpD renders Pseudomonas aeruginosa unable to establish a lethal systemic infection, associated with enhanced bacterial clearance in vivo. CbpD-dependent survival of the wild-type bacterium is not attributable to dampening of pro-inflammatory responses by CbpD ex vivo or in vivo. CbpD attenuates the terminal complement cascade in human serum. Catalytic activity is crucial for virulence function. The lack of the enzyme result in substantial reorganization of the bacterial and host proteomes
physiological function
-
LPMO10 and a chitinase mutually enhance each others activities upon degrading chitin as the substrate
-
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
-
deletion of cbpD renders Pseudomonas aeruginosa unable to establish a lethal systemic infection, associated with enhanced bacterial clearance in vivo. CbpD-dependent survival of the wild-type bacterium is not attributable to dampening of pro-inflammatory responses by CbpD ex vivo or in vivo. CbpD attenuates the terminal complement cascade in human serum. Catalytic activity is crucial for virulence function. The lack of the enzyme result in substantial reorganization of the bacterial and host proteomes
-
physiological function
-
presence of LPMO10 increases the rate of chitin depolymerization by both chitinases ChiA and ChiB
-
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
-
enzyme produces oxidized cello-oligosaccharides from cellulose and boosts cellulose degradation by cellulases. The binding ability of LPMO10A depends on carbohydrate binding module CBM2
-
physiological function
Fusarium fujikuroi CBS 195.34
-
member of lytic polysaccharide monooxygenase family AA11
-
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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). LCHMO_STRA7
Streptomyces ambofaciens (strain ATCC 23877 / 3486 / DSM 40053 / JCM 4204 / NBRC 12836 / NRRL B-2516)
172
1
17827
Swiss-Prot
-
LCHMO_ENTFA
Enterococcus faecalis (strain ATCC 700802 / V583)
194
1
21138
Swiss-Prot
-
A0A0C5K362_BACTK
221
0
24148
TrEMBL
-
B1VN59_STRGG
Streptomyces griseus subsp. griseus (strain JCM 4626 / CBS 651.72 / NBRC 13350 / KCC S-0626 / ISP 5235)
171
0
17864
TrEMBL
-
B1VNK5_STRGG
Streptomyces griseus subsp. griseus (strain JCM 4626 / CBS 651.72 / NBRC 13350 / KCC S-0626 / ISP 5235)
360
0
37668
TrEMBL
-
C7R4I0_JONDD
Jonesia denitrificans (strain ATCC 14870 / DSM 20603 / BCRC 15368 / CIP 55.134 / JCM 11481 / NBRC 15587 / NCTC 10816 / Prevot 55134)
651
1
69349
TrEMBL
Mitochondrion (Reliability: 3)
LP11_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
421
0
42628
Swiss-Prot
other Location (Reliability: 4)
Q3JY22_BURP1
Burkholderia pseudomallei (strain 1710b)
214
0
24019
TrEMBL
-
LP11A_ASPFU
Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)
219
0
23539
Swiss-Prot
other Location (Reliability: 1)
Q62YN7_BACLD
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46)
203
0
22656
TrEMBL
other Location (Reliability: 3)
Q8Y4H4_LISMO
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
478
0
52271
TrEMBL
-
CBPD_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
389
0
41917
Swiss-Prot
-
Q9RJC1_STRCO
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
228
0
25168
TrEMBL
-
S0DX13_GIBF5
Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831)
404
0
40914
TrEMBL
other Location (Reliability: 4)
V5N5H9_STRCO
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
134
0
14620
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 20000, SDS-PAGE, x * 20540, calculated
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
sequence contains a possible N-glycosylation site, at Asn62. Treatment with endo-beta-N-acetylglucosaminidase leads to a mass reduction to 22 kDA
glycoprotein
-
sequence contains a possible N-glycosylation site, at Asn62. Treatment with endo-beta-N-acetylglucosaminidase leads to a mass reduction to 22 kDA
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling reveals the typical central beta-sandwich fold of LPMOs, as well as flexible loops and two stabilizing disulfide bonds. The active site contains the histidine brace, consisting of His1 and His96 coordinating the copper cofactor, and the axial, non-coordinating residue Phe187
-
structure shows a substrate-binding surface with features similar to known chitin-active LPMOs and the absence of a carbohydrate-binding module
in presence of Zn2+, to 1.55 A resolution, and in presence of Cu2+, to 1.4 AS resolution
solution-phase structure of apo-LPMO10A and of Cu(I)-LPMO10A. The presence of the metal has minimal effects on the overall protein structure. Large changes in the Cu(II) spin-Hamiltonian parameters are induced upon binding of the substrate. Changes arise from a rearrangement of the copper coordination sphere from a five-coordinate distorted square pyramid to a four-coordinate near-square planar
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
to 1.85 A resolution, tri-modular enzyme containing a catalytic family AA10 LPMO module, a family 5 chitin-binding module, and a C-terminal unclassified module which displays tight and specific binding to chitin
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
crystal structure in the Cu(II)-bound form and photoreduction of the crystalline protein in the x-ray beam, leading to conversion from the initial Cu(II)-oxidized form with two coordinated water molecules, which adopts a trigonal bipyramidal geometry, to a reduced Cu(I) form in a T-shaped geometry with no coordinated water molecules
1.1 A resolution room-temperature X-ray structure and 2.1 A resolution neutron structure, show a putative dioxygen species equatorially bound to the active site copper with elongated density for the dioxygen, most consistent with a Cu(II)-bound peroxide
1.55 A resolution structure of N-terminal LPMO10A module reveals deletions of interacting loops that protrude from the core beta-sandwich scaffold in larger LPMO10s
structure of the catalytic domain (residues 37-230, lacking the linker and the CBM2) to 1.08 A resolution. Structure shows the typical LPMO fold with a central beta-sandwich made up by two distorted beta-sheets connected by several loops and helices. The active site is formed by His37 and His144 that coordinate the copper atom in a T-shaped geometry
D9SZQ3
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
D9SZQ3
structures in the resting state and of a copper(II)-dioxo intermediate complex formed in the absence of substrate reveal pre-bound molecular oxygen adjacent to the active site. A conserved histidine is involved in promoting oxygen activation
to 1.2 A resolution. Diffraction resolution and crystal morphology are improved by expression from a glycoengineered strain of Pichia pastoris
crystallization at pH 3.5. Structure shows shows significant disorder of the active site in the absence of substrate ligand
homology modeling and molecular docking, a binding site for the chitin heptamer exists near the histidine brace active site
homology modeling, CbpD is a monomeric tri-modular enzyme with flexible linkers
calculation of solution structure. Ca2+, Mg2+, Fe3+, Co2+, Zn2+, or Cu2+ ions show binding to an interaction site located between His28 and His114
molecular dynamics interactions between the LPMO and three different surface topologies of crystalline chitin. Most enzyme-substrate interactions involve the polysaccharide chain that is to be cleaved. Enzyme displays a constrained active site geometry as well as a tunnel connecting the bulk solvent to the copper site, through which only small molecules such as H2O, O2, and H2O2 can diffuse. Rearrangement of Cu-coordinating water molecules is necessary when binding the substrate and also provide a rationale for the experimentally observed C1 oxidative regiospecificity
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
homology modeling. Residues His1 and His61 directly coordinate the basic copper cofactor in T-shaped geometry. The axial, noncoordinating active site residue is Tyr142
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D140A
D9SZQ3
mutant shows moderately reduced activity and essentially unchanged oxidative regioselectivity
N85F
D9SZQ3
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.9
W82Y
D9SZQ3
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 2.0
W82Y/N85F
D9SZQ3
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 10.9
W82Y/N85F/Q141W
W82Y/N85F/Y116F
D9SZQ3
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 14.7
W82Y/N85F/Y116F/Q141W
D140A
Micromonospora aurantiaca (nom. illeg.) DSM 43813
-
mutant shows moderately reduced activity and essentially unchanged oxidative regioselectivity
-
N85F
Micromonospora aurantiaca (nom. illeg.) DSM 43813
-
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.9
-
W82Y
Micromonospora aurantiaca (nom. illeg.) DSM 43813
-
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 2.0
-
Y54A
mutation of residue at subsite -4, minimal effect on degradation of beta-chitin, about 20% residual activity with substrate [(1->4)-N-acetyl-beta-D-glucosaminyl]6
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
N80D/F82A/Y111F/W141Q
mutations of the substrate-binding surface, decreases thermal stability. Mutant is exclusively C1-oxidizing and displays activity on chitin and cellulose
W88Y/N91F
mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54
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
-
Y56W
H1A
hydrogen bonds between the copper ion and the predicted active site residues are similar to wild-type
H61A
distance between the copper ion and the predicted active site residue are increased
Y142A
distance between the copper ion and the predicted active site residue are increased
H1A
Trichoderma guizhouense NJAU 47420
-
hydrogen bonds between the copper ion and the predicted active site residues are similar to wild-type
-
H61A
Trichoderma guizhouense NJAU 47420
-
distance between the copper ion and the predicted active site residue are increased
-
Y142A
Trichoderma guizhouense NJAU 47420
-
distance between the copper ion and the predicted active site residue are increased
-
additional information
W82Y/N85F/Q141W
D9SZQ3
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.1
W82Y/N85F/Q141W
D9SZQ3
loss of chitin monooxygenase activity, 12.21% residual cellulose C1- and 2.1% residual C4-oxidizing activity, ratio C1:C4-activity is 5.06
W82Y/N85F/Y116F/Q141W
D9SZQ3
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.8
W82Y/N85F/Y116F/Q141W
D9SZQ3
loss of chitin oxidizinbg activity, 10.2% residual cellulose C1- and 1.6% residual C4-oxidizing activity, ratio C1:C4-activity is 5.78
Y56W
mutation shows no detectable effect on substrate-binding preferences but, in synergy experiments with chitinases, the mutant appears to be more efficient on alpha-chitin
Y56W
-
mutation shows no detectable effect on substrate-binding preferences but, in synergy experiments with chitinases, the mutant appears to be more efficient on alpha-chitin
-
additional information
removal of the chitin-binding modules reduces LPMO activity toward alpha-chitin. The full-length enzyme and the individual catalytic LPMO module boost the activity of an endochitinase equally well
additional information
D9SZQ3
neither truncation of theLPMO10B family 2 carbohydrate-binding module nor mutations altering access to the solvent-exposed axial copper coordination site significantly change the C1:C4 oxidation ratio
additional information
Micromonospora aurantiaca (nom. illeg.) DSM 43813
-
neither truncation of theLPMO10B 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
additional information
additional information
-
chitin binding increases the thermal stability of the enzyme by 8.3 degrees, copper binding increases melting temperature by 21.6 degrees. Addition of chitin to the copper-bound enzyme increases thermal stability by additional 3.5 degrees
additional information
thermal unfolding of both apo- and holoCBP21 is reversible. ApoCBP21 unfolds in a simple two-state transition manner. The peak temperature of the differential scanning calorimetry curve, tp, for holoCBP21is (74.4°C and that for apoCBP21 is 65.6°C). HoloCBP21 is stabilized by 35 kJ/mol in terms of the Gibbs energy change for unfolding (pH 5.0, 25°C), compared with apoCBP21
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression Bacillus subtilis yields a simple purification process without complicated periplasmic fractionation, as well as improved productivity
A0A0H3E2X6
improved expression and purification protocol using Champion pET-SUMO vector, yielding high purity AA10 with yields in excess of 9 mg of protein per litre of culture
-
protocol for cloning, expression and purification of lytic cellulose monooxygenase (EC 1.14.99.54) and lytic chitin monooxygenase (EC 1.14.99.53), especially from termites, silkworm and honeybee
-
simple purification method by affinity adsorption to obtain functional lytic polysaccharide monooxygenases. Purification follows a binding-elution protocol with low-grade polysaccharides including Avicel
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Pichia pastoris
expression using a Brevibacillus-based expression system
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
during the course of melon infection, host and pathogen genes present similar expression patterns. Host endochitinases and LPMO1 are coexpressed during the first stages of expression
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
degradation
synthesis
analysis
-
method for quantification of C1-oxidized chitooligosaccharides (aldonic acids), and hence LPMO activity
analysis
A0A0H3E2X6
development of a chitinase-coupled assay method and an assay based on consumption of ascorbate. There is no H2O2 production in the presence of colloidal chitin at 4 mg/ml
analysis
-
method to kinetically assess the cellulolytic peroxygenase reaction using competition between well characterized reference enzymes and LPMOs for the H2O2 cosubstrate. LPMOs of both bacterial and fungal origin showed high peroxygenase efficiencies, with kcat/KmH2O2 values in the order of 100-1000 mM/s
analysis
-
method to kinetically assess the cellulolytic peroxygenase reaction using competition between well characterized reference enzymes and LPMOs for the H2O2 cosubstrate. LPMOs of both bacterial and fungal origin showed high peroxygenase efficiencies, with kcat/KmH2O2 values in the order of 100-1000 mM/s
analysis
-
development of a chitinase-coupled assay method and an assay based on consumption of ascorbate. There is no H2O2 production in the presence of colloidal chitin at 4 mg/ml
-
degradation
presence of lytic polysaccharide monooxygenase CBP21 facilitates the degradation of chitin substrates (colloidal chitin, beta-chitin, and alpha-chitin) by Chi92
degradation
under optimised conditions, AA11 introduces 35 nmol of carboxylate moieties per milligram of alpha-chitin. AA11 accepts lobster shells as substrate. The use of ethyl(hydroxyimino)cyanoacetate (Oxyma) assisted click chemistry allows the rapid modification of the surface of AA11-oxidized chitins, with a fluorescent probe, a peptide, and gold nanoparticles
degradation
Fusarium fujikuroi CBS 195.34
-
under optimised conditions, AA11 introduces 35 nmol of carboxylate moieties per milligram of alpha-chitin. AA11 accepts lobster shells as substrate. The use of ethyl(hydroxyimino)cyanoacetate (Oxyma) assisted click chemistry allows the rapid modification of the surface of AA11-oxidized chitins, with a fluorescent probe, a peptide, and gold nanoparticles
-
synthesis
-
construction of a cassette vector containing the XylS/Pm system that can easily be used for exchanging LPMO coding genes with or without signal sequences. The cassette reliably produces mature (translocated) LPMOs under controlled conditions. The signal sequence of LPMO10A from Serratia marcescens gives highest levels of recombinant protein production and translocation
synthesis
efficient production in Escherichia coli is achieved using PelB as the most productive signal peptide for the extracellular production of CBP21 and Aeromonas veronii B565 chitinase Chi92
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Duzhak, A.B.; Panfilova, Z.I.; Duzhak, T.G.; Vasyunina, E.A.
Extracellular chitinases of mutant superproducing strain Serratia marcescens M-1
Biochemistry (Moscow)
74
209-214
2009
Serratia marcescens (O83009)
brenda
Zhang, H.; Zhao, Y.; Cao, H.; Mou, G.; Yin, H.
Expression and characterization of a lytic polysaccharide monooxygenase from Bacillus thuringiensis
Int. J. Biol. Macromol.
79
72-75
2015
Bacillus thuringiensis (A0A0C5K362), Bacillus thuringiensis ACCC 10066 (A0A0C5K362), Bacillus thuringiensis serovar kurstaki (A0A0C5K362), Bacillus thuringiensis serovar kurstaki ACCC 10066 (A0A0C5K362)
brenda
Gudmundsson, M.; Kim, S.; Wu, M.; Ishida, T.; Momeni, M.H.; Vaaje-Kolstad, G.; Lundberg, D.; Royant, A.; Stahlberg, J.; Eijsink, V.G.; Beckham, G.T.; Sandgren, M.
Structural and electronic snapshots during the transition from a Cu(II) to Cu(I) metal center of a lytic polysaccharide monooxygenase by X-ray photoreduction
J. Biol. Chem.
289
18782-18792
2014
Enterococcus faecalis (Q838S1)
brenda
Vaaje-Kolstad, G.; Bohle, L.A.; Gaseidnes, S.; Dalhus, B.; Bjoras, M.; Mathiesen, G.; Eijsink, V.G.
Characterization of the chitinolytic machinery of Enterococcus faecalis V583 and high-resolution structure of its oxidative CBM33 enzyme
J. Mol. Biol.
416
239-254
2012
Enterococcus faecalis (Q838S1)
brenda
Vaaje-Kolstad, G.; Westereng, B.; Horn, S.J.; Liu, Z.; Zhai, H.; Sorlie, M.; Eijsink, V.G.
An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides
Science
330
219-222
2010
Serratia marcescens (O83009)
brenda
O'Dell, W.; Swartz, P.; Weiss, K.; Meilleur, F.
Crystallization of a fungal lytic polysaccharide monooxygenase expressed from glycoengineered Pichia pastoris for X-ray and neutron diffraction
Acta Crystallogr. Sect. F
73
70-78
2017
Neurospora crassa (Q8WZQ2)
brenda
ODell, W.B.; Agarwal, P.K.; Meilleur, F.
Oxygen activation at the active site of a fungal lytic polysaccharide monooxygenase
Angew. Chem. Int. Ed. Engl.
56
767-770
2017
Neurospora crassa (Q8WZQ2)
brenda
Bacik, J.P.; Mekasha, S.; Forsberg, Z.; Kovalevsky, A.Y.; Vaaje-Kolstad, G.; Eijsink, V.G.H.; Nix, J.C.; Coates, L.; Cuneo, M.J.; Unkefer, C.J.; Chen, J.C.
Neutron and atomic resolution X-ray structures of a lytic polysaccharide monooxygenase reveal copper-mediated dioxygen binding and evidence for N-terminal deprotonation
Biochemistry
56
2529-2532
2017
Jonesia denitrificans (C7R4I0), Jonesia denitrificans DSM 20603 (C7R4I0)
brenda
Book, A.; Yennamalli, R.; Takasuka, T.; Currie, C.; Phillips, G.; Fox, B.
Evolution of substrate specificity in bacterial AA10 lytic polysaccharide monooxygenases
Biotechnol. Biofuels
7
109
2014
Burkholderia pseudomallei (Q3JY22), Burkholderia pseudomallei 1710b (Q3JY22), Enterococcus faecalis (Q838S1), Enterococcus faecalis ATCC 700802 (Q838S1)
brenda
Hamre, A.G.; Eide, K.B.; Wold, H.H.; Sorlie, M.
Activation of enzymatic chitin degradation by a lytic polysaccharide monooxygenase
Carbohydr. Res.
407
166-169
2015
Serratia marcescens (O83009)
brenda
Frandsen, K.E.; Poulsen, J.N.; Tandrup, T.; Lo Leggio, L.
Unliganded and substrate bound structures of the cellooligosaccharide active lytic polysaccharide monooxygenase LsAA9A at low pH
Carbohydr. Res.
448
187-190
2017
Panus similis (A0A0S2GKZ1)
brenda
Gregory, R.C.; Hemsworth, G.R.; Turkenburg, J.P.; Hart, S.J.; Walton, P.H.; Davies, G.J.
Activity, stability and 3-D structure of the Cu(II) form of a chitin-active lytic polysaccharide monooxygenase from Bacillus amyloliquefaciens
Dalton Trans.
45
16904-16912
2016
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens DSM 7
brenda
Yu, M.J.; Yoon, S.H.; Kim, Y.W.
Overproduction and characterization of a lytic polysaccharide monooxygenase in Bacillus subtilis using an assay based on ascorbate consumption
Enzyme Microb. Technol.
93-94
150-156
2016
Bacillus atrophaeus (A0A0H3E2X6), Bacillus atrophaeus 1942 (A0A0H3E2X6)
brenda
Nakagawa, Y.S.; Kudo, M.; Loose, J.S.; Ishikawa, T.; Totani, K.; Eijsink, V.G.; Vaaje-Kolstad, G.
A small lytic polysaccharide monooxygenase from Streptomyces griseus targeting alpha- and beta-chitin
FEBS J.
282
1065-1079
2015
Streptomyces griseus subsp. griseus (B1VN59), Streptomyces griseus subsp. griseus JCM 4626 (B1VN59)
brenda
Paspaliari, D.K.; Loose, J.S.; Larsen, M.H.; Vaaje-Kolstad, G.
Listeria monocytogenes has a functional chitinolytic system and an active lytic polysaccharide monooxygenase
FEBS J.
282
921-936
2015
Listeria monocytogenes serotype 1/2a (Q8Y4H4), Listeria monocytogenes serotype 1/2a ATCC BAA-679 (Q8Y4H4)
brenda
Loose, J.; Forsberg, Z.; Fraaije, M.; Eijsink, V.; Vaaje-Kolstad, G.
A rapid quantitative activity assay shows that the Vibrio cholerae colonization factor GbpA is an active lytic polysaccharide monooxygenase
FEBS Lett.
588
3435-3440
2014
Vibrio cholerae serotype O1
brenda
Mekasha, S.; Forsberg, Z.; Dalhus, B.; Bacik, J.P.; Choudhary, S.; Schmidt-Dannert, C.; Vaaje-Kolstad, G.; Eijsink, V.G.
Structural and functional characterization of a small chitin-active lytic polysaccharide monooxygenase domain of a multi-modular chitinase from Jonesia denitrificans
FEBS Lett.
590
34-42
2016
Jonesia denitrificans (C7R4I0), Jonesia denitrificans DSM 20603 (C7R4I0)
brenda
Nakagawa, Y.S.; Eijsink, V.G.; Totani, K.; Vaaje-Kolstad, G.
Conversion of alpha-chitin substrates with varying particle size and crystallinity reveals substrate preferences of the chitinases and lytic polysaccharide monooxygenase of Serratia marcescens
J. Agric. Food Chem.
61
11061-11066
2013
Serratia marcescens (O83009)
brenda
Forsberg, Z.; Nelson, C.E.; Dalhus, B.; Mekasha, S.; Loose, J.S.; Crouch, L.I.; Rohr, A.K.; Gardner, J.G.; Eijsink, V.G.; Vaaje-Kolstad, G.
Structural and functional analysis of a lytic polysaccharide monooxygenase important for efficient utilization of chitin in Cellvibrio japonicus
J. Biol. Chem.
291
7300-7312
2016
Cellvibrio japonicus (B3PJ79)
brenda
Hemsworth, G.R.; Henrissat, B.; Davies, G.J.; Walton, P.H.
Discovery and characterization of a new family of lytic polysaccharide monooxygenases
Nat. Chem. Biol.
10
122-126
2014
Aspergillus oryzae (Q2UA85), Aspergillus oryzae ATCC 42149 (Q2UA85)
brenda
Aachmann, F.; Sorlie, M.; Skjak-Brak, G.; Eijsink, V.; Vaaje-Kolstad, G.
NMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactions
Proc. Natl. Acad. Sci. USA
109
18779-18784
2012
Serratia marcescens (O83009)
brenda
Forsberg, Z.; Mackenzie, A.; Sorlie, M.; Rohr, A.; Helland, R.; Arvai, A.; Vaaje-Kolstad, G.; Eijsink, V.
Structural and functional characterization of a conserved pair of bacterial cellulose-oxidizing lytic polysaccharide monooxygenases
Proc. Natl. Acad. Sci. USA
111
8446-8451
2014
Streptomyces coelicolor (Q9RJC1), Streptomyces coelicolor ATCC BAA-471 (Q9RJC1)
brenda
Loose, J.S.; Forsberg, Z.; Kracher, D.; Scheiblbrandner, S.; Ludwig, R.; Eijsink, V.G.; Vaaje-Kolstad, G.
Activation of bacterial lytic polysaccharide monooxygenases with cellobiose dehydrogenase
Protein Sci.
25
2175-2186
2016
Streptomyces coelicolor (V5N5H9), Streptomyces coelicolor ATCC BAA-471 (V5N5H9)
brenda
Yang, Y.; Li, J.; Liu, X.; Pan, X.; Hou, J.; Ran, C.; Zhou, Z.
Improving extracellular production of Serratia marcescens lytic polysaccharide monooxygenase CBP21 and Aeromonas veronii B565 chitinase Chi92 in Escherichia coli and their synergism
AMB Express
7
170
2017
Serratia marcescens (O83009)
brenda
Bissaro, B.; Isaksen, I.; Vaaje-Kolstad, G.; Eijsink, V.; Rohr, A.
How a lytic polysaccharide monooxygenase binds crystalline chitin
Biochemistry
57
1893-1906
2018
Serratia marcescens (O83009)
brenda
Valenzuela, S.; Ferreres, G.; Margalef, G.; Pastor, F.
Fast purification method of functional LPMOs from Streptomyces ambofaciens by affinity adsorption
Carbohydr. Res.
448
205-211
2017
Streptomyces ambofaciens
brenda
Courtade, G.; Le, S.; Satrom, G.; Brautaset, T.; Aachmann, F.
A novel expression system for lytic polysaccharide monooxygenases
Carbohydr. Res.
448
212-219
2017
Serratia marcescens
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 (nom. illeg.) (D9SZQ3), Micromonospora aurantiaca (nom. illeg.) DSM 43813 (D9SZQ3), Streptomyces coelicolor (Q9RJC1), Streptomyces coelicolor ATCC BAA-471 (Q9RJC1)
brenda
Sabbadin, F.; Henrissat, B.; Bruce, N.; McQueen-Mason, S.
Lytic polysaccharide monooxygenases as chitin-specific virulence factors in crayfish plague
Biomolecules
11
1180
2021
Aphanomyces astaci
brenda
Sugimoto, H.; Nakajima, Y.; Motoyama, A.; Katagiri, E.; Watanabe, T.; Suzuki, K.
Unfolding of CBP21, a lytic polysaccharide monooxygenase, without dissociation of its copper ion cofactor
Biopolymers
111
e23339
2020
Serratia marcescens (O83009)
brenda
Li, F.; Liu, Y.; Liu, Y.; Li, Y.; Yu, H.
Heterologous expression and characterization of a novel lytic polysaccharide monooxygenase from Natrialbaceae archaeon and its application for chitin biodegradation
Biores. Technol.
354
127174
2022
Natrialbaceae
brenda
Ma, L.; Liu, Z.; Kong, Z.; Wang, M.; Li, T.; Zhu, H.; Wan, Q.; Liu, D.; Shen, Q.
Functional characterization of a novel copper-dependent lytic polysaccharide monooxygenase TgAA11 from Trichoderma guizhouense NJAU 4742 in the oxidative degradation of chitin
Carbohydr. Polym.
258
117708
2021
Trichoderma guizhouense (A0A1T3C909), Trichoderma guizhouense NJAU 47420 (A0A1T3C909)
brenda
Wang, D.; Li, J.; Salazar-Alvarez, G.; McKee, L.; Srivastava, V.; Sellberg, J.; Bulone, V.; Hsieh, Y.
Production of functionalised chitins assisted by fungal lytic polysaccharide monooxygenase
Green Chem.
20
2091-2100
2018
Fusarium fujikuroi (S0DX13), Fusarium fujikuroi CBS 195.34 (S0DX13)
-
brenda
Qu, M.; Guo, X.; Kong, L.; Hou, L.; Yang, Q.
A midgut-specific lytic polysaccharide monooxygenase of Locusta migratoria is indispensable for the deconstruction of the peritrophic matrix
Insect Sci.
29
1287-1298
2022
Locusta migratoria
brenda
Sato, K.; Chiba, D.; Yoshida, S.; Takahashi, M.; Totani, K.; Shida, Y.; Ogasawara, W.; Nakagawa, Y.S.
Functional analysis of a novel lytic polysaccharide monooxygenase from Streptomyces griseus on cellulose and chitin
Int. J. Biol. Macromol.
164
2085-2091
2020
Streptomyces griseus subsp. griseus (B1VNK5), Streptomyces griseus subsp. griseus JCM 4626 (B1VNK5)
brenda
Jensen, M.S.; Klinkenberg, G.; Bissaro, B.; Chylenski, P.; Vaaje-Kolstad, G.; Kvitvang, H.F.; Naerdal, G.K.; Sletta, H.; Forsberg, Z.; Eijsink, V.G.H.
Engineering chitinolytic activity into a cellulose-active lytic polysaccharide monooxygenase provides insights into substrate specificity
J. Biol. Chem.
294
19349-19364
2019
Streptomyces coelicolor (V5N5H9)
brenda
Madland, E.; Forsberg, Z.; Wang, Y.; Lindorff-Larsen, K.; Niebisch, A.; Modregger, J.; Eijsink, V.G.H.; Aachmann, F.L.; Courtade, G.
Structural and functional variation of chitin-binding domains of a lytic polysaccharide monooxygenase from Cellvibrio japonicus
J. Biol. Chem.
297
101084
2021
Cellvibrio japonicus (B3PJ79), Cellvibrio japonicus Ueda107 (B3PJ79)
brenda
Stopamo, F.; Rohr, A.; Mekasha, S.; Petrovi, D.; Varnai, A.; Eijsink, V.
Characterization of a lytic polysaccharide monooxygenase from Aspergillus fumigatus shows functional variation among family AA11 fungal LPMOs
J. Biol. Chem.
297
101421
2021
Aspergillus fumigatus (Q4WF00), Aspergillus fumigatus ATCC MYA-4609 (Q4WF00)
brenda
Arora, R.; Bharval, P.; Sarswati, S.; Sen, T.; Yennamalli, R.
Structural dynamics of lytic polysaccharide monoxygenases reveals a highly flexible substrate binding region
J. Mol. Graph. Model.
88
1-10
2019
Bacteria
brenda
Polonio, A.; Fernandez-Ortuno, D.; de Vicente, A.; Perez-Garcia, A.
A haustorial-expressed lytic polysaccharide monooxygenase from the cucurbit powdery mildew pathogen Podosphaera xanthii contributes to the suppression of chitin-triggered immunity
Mol. Plant Pathol.
22
580-601
2021
Podosphaera xanthii (A0A8E4PV92)
brenda
Kont, R.; Bissaro, B.; Eijsink, V.; Vaeljamaee, P.
Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)
Nat. Commun.
11
5786
2020
Serratia marcescens, Streptomyces coelicolor
brenda
Askarian, F.; Uchiyama, S.; Masson, H.; Sorensen, H.; Golten, O.; Bunaes, A.; Mekasha, S.; Rohr, A.; Kommedal, E.; Ludviksen, J.; Arntzen, M.; Schmidt, B.; Zurich, R.; van Sorge, N.; Eijsink, V.; Krengel, U.; Mollnes, T.; Lewis, N.; Nizet, V.; Vaaje-Kol, G.
The lytic polysaccharide monooxygenase CbpD promotes Pseudomonas aeruginosa virulence in systemic infection
Nat. Commun.
12
1230
2021
Pseudomonas aeruginosa (Q9I589), Pseudomonas aeruginosa DSM 22644 (Q9I589)
brenda
Courtade, G.; Ciano, L.; Paradisi, A.; Lindley, P.J.; Forsberg, Z.; Sorlie, M.; Wimmer, R.; Davies, G.J.; Eijsink, V.G.H.; Walton, P.H.; Aachmann, F.L.
Mechanistic basis of substrate-O2 coupling within a chitin-active lytic polysaccharide monooxygenase An integrated NMR/EPR study
Proc. Natl. Acad. Sci. USA
117
19178-19189
2020
Bacillus licheniformis (Q62YN7), Bacillus licheniformis DSM 13 (Q62YN7)
brenda
Franco Cairo, J.; Almeida, D.; Damasio, A.; Garcia, W.; Squina, F.
The periplasmic expression and purification of AA15 lytic polysaccharide monooxygenases from insect species in Escherichia coli
Protein Expr. Purif.
190
105994
2022
Arthropoda
brenda
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