1.14.99.53: lytic chitin monooxygenase
This is an abbreviated version!
For detailed information about lytic chitin monooxygenase, go to the full flat file.
Word Map on EC 1.14.99.53
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1.14.99.53
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polysaccharide
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chitinases
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lpmos
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recalcitrant
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chitinolytic
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cellulose
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biomass
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c1-oxidizer
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analysis
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synthesis
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listeria
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transposon
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monocytogenes
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degradation
- 1.14.99.53
- polysaccharide
- chitinases
-
lpmos
-
recalcitrant
-
chitinolytic
- cellulose
- biomass
-
c1-oxidizer
- analysis
- synthesis
-
listeria
- transposon
- monocytogenes
- degradation
Reaction
Synonyms
AA10, AA10A, AA9A, AO090102000501, BATR1942_08650, BURPS1710b_0114, CBM33A, CBP21, Cbp33A, CelS2, chitin-binding domain 3 protein, EF_0362, G15G9.090, GbpA, Jden_1381, lmo2467, LPMO10, LPMO10A, LPMO10B, LPMO10F, Micau_1630, PMO-2, RBAM17540, SCO0643, SGR_6855
ECTree
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Metals Ions
Metals Ions on EC 1.14.99.53 - lytic chitin monooxygenase
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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+
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+
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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