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Information on EC 1.14.99.53 - lytic chitin monoxygenase Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The enzyme appears in viruses and cellular organisms
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lytic chitin monoxygenase
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(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
(1) the initially formed D-glucono-1,5-lactone at the reducing end of the chitin chain quickly hydrolyzes spontaneously to the aldonic acid
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(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
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chitin degradation III (Serratia)
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chitin, hydrogen-donor:oxygen oxidoreductase (N-acetyl-beta-D-glucosaminyl C1-hydroxylating/C4-dehdrogenating)
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EF_0362
gene name
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subsp. Kurstaki
UniProt
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subsp. Kurstaki
UniProt
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UniProt
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UniProt
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chitin + acceptor + O2
[chitin oligosaccharide]-N-acetyl-D-glucosaminate + [chitin oligosaccharide]-N-acetyl-D-glucosamino-1,5-lactone
chitin + acceptor + O2
[chitin oligosaccharide]-N-acetyl-D-glucosaminate + [chitin oligosaccharide]-N-acetyl-D-glucosamino-1,5-lactone
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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.
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chitin + acceptor + O2
[chitin oligosaccharide]-N-acetyl-D-glucosaminate + [chitin oligosaccharide]-N-acetyl-D-glucosamino-1,5-lactone
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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.
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Cu2+
dependent on
Cu2+
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structure of the copper-binding site
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brenda
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21000
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x * 21000, SDS-PAGE
24150
calculated from amino acid sequence
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expressed in Escherichia coli BL21
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A0A0C5K362_BACTK
221
24148
TrEMBL
O83009_SERMA
197
21586
TrEMBL
Q838S1_ENTFA
Enterococcus faecalis (strain ATCC 700802 / V583)
194
21138
TrEMBL
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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), Serratia marcescens
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)
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
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