1.14.99.54: lytic cellulose monooxygenase (C1-hydroxylating)
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For detailed information about lytic cellulose monooxygenase (C1-hydroxylating), go to the full flat file.
Word Map on EC 1.14.99.54
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1.14.99.54
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lpmos
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recalcitrant
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lignocellulosic
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copper-dependent
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chitinases
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cellulases
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chitinolytic
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saccharification
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biorefinery
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chitin-active
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cellobiohydrolases
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cellulose-active
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carbohydrate-active
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thermoascus
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degradation
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cello-oligosaccharides
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c1-oxidizing
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endoglucanases
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avicel
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analysis
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chic
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monocopper
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synthesis
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chitin-degrading
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beta-chitin
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aldonic
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myceliophthora
- 1.14.99.54
-
lpmos
-
recalcitrant
-
lignocellulosic
-
copper-dependent
- chitinases
- cellulases
-
chitinolytic
-
saccharification
-
biorefinery
-
chitin-active
- cellobiohydrolases
-
cellulose-active
-
carbohydrate-active
-
thermoascus
- degradation
- cello-oligosaccharides
-
c1-oxidizing
- endoglucanases
- avicel
- analysis
-
chic
-
monocopper
- synthesis
-
chitin-degrading
- beta-chitin
-
aldonic
-
myceliophthora
Reaction
Synonyms
AA13, AA14A, AA14B, AA9, AA9 LPMO, AA9A, AO090701000246, CBP21, Cel61a, cel61b, Cel7A, CelS2, chitin-binding domain 3 protein, endoglucanase II, endoglucanase IV, FG02202.1, GbpA, Gh61 isozyme a, gh61-4, gh61-5, GH61D, gh61e, GH61H, LPMO, LPMO-02916, LPMO10A, LPMO10B, LPMO10C, LPMO9A, LPMO9B, LPMO9C, LPMO9D, LPMO9E, LPMO9f, Lpmo9H, lytic polysaccharide monooxygenase, Micau_1630, NCU01050, NCU07898, PaGH61A, PaGH61B, PMO, PMO-2, PMO-3, PODANS_2_6530, PODANS_7_3160, polysaccharide monoxygenase, PsLPMOA, PsLPMOB, Pte6, SCO0643, SCO1188, Tfu_1268, Tfu_1665
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Metals Ions
Metals Ions on EC 1.14.99.54 - lytic cellulose monooxygenase (C1-hydroxylating)
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Cu2+
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+
The copper ion lies in the center of a flat surface that interacts with the substrate. The equatorial plane includes the protein's N-terminal Ndelta of His-1 and the Nepsilon of His-83
Cu2+
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the reduction of the mononuclear active-site copper by ascorbic acid increases the affinity and the maximum binding capacity of LPMO for cellulose
Cu2+
the calculated dissociation energies suggest that the reactive intermediate is either a Cu(II)-oxyl, a Cu(III)-oxyl, or a Cu(III)-hydroxide, indicating that O-O bond breaking occurs before the C-H activation step
Cu2+
KR825269, KR825270
strictly conserved copper-binding site which consists of two histidines (one at N-terminal position) and one tyrosine
Cu2+
type II copper center, which exhibits a hexacoordination
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
Cu2+
the copper site of CelS2 is similar to that of chitin-active LPMO10s. Dissociation constant is 31 nM
Cu2+
EDTA-inhibited enzyme can be reactivated by 20 mM Cu2+ within 1 h
Cu2+
enzyme is Cu(II) saturated with a 3fold molar excess of Cu(II)SO4 prior to assay
Cu2+
the oxidized catalytic center contains a Cu(II) coordinated by two His ligands, one of which has a His-brace in which the His-1 terminal amine group also coordinates to a copper. The final equatorial position of the Cu(II) is occupied by a water-derived ligand