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
1.14.99.53 lytic chitin monooxygenaseAdvanced search results
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results (Engineering
Engineering on EC 1.14.99.53 - lytic chitin monooxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D140A
mutant shows moderately reduced activity and essentially unchanged oxidative regioselectivity
N85F
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.9
W82Y
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 2.0
W82Y/N85F
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 10.9
W82Y/N85F/Q141W
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.1
W82Y/N85F/Y116F
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 14.7
W82Y/N85F/Y116F/Q141W
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.8
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
W88Y/N91F
mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54
A148G
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mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54
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A148S
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mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54
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Y56W
additional information
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
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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
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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
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
