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Information on EC 1.14.99.53 - lytic chitin monooxygenase

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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.
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This record set is specific for:
UNIPROT: O83009
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
lpmo10, lmo2467, lytic chitin monooxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
(1) the initially formed D-glucono-1,5-lactone at the reducing end of the chitin chain quickly hydrolyzes spontaneously to the aldonic acid
PATHWAY SOURCE
PATHWAYS
-
-, -
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-chitin + ascorbate + O2
oxidized chitooligosaccharides + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
beta-chitin + ascorbate + O2
C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
chitin + acceptor + O2
? + reduced acceptor + H2O
show the reaction diagram
-
-
-
?
[(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
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
Kd value 55 nM, from isothermal titration calorimetry, and for Cu1+, Kd value 1 nM from the experimentally determined redox potential
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+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cyanide
mimic of molecular oxygen, binds to the metal ion only
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O83009_SERMA
197
0
21586
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21000
x * 21000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 21000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
presence of lytic polysaccharide monooxygenase CBP21 facilitates the degradation of chitin substrates (colloidal chitin, beta-chitin, and alpha-chitin) by Chi92
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
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team