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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General Information
General Information on EC 1.14.99.53 - lytic chitin monooxygenase
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physiological function
cellobiose dehydrogenase from Myriococcum thermophilum can act as an electron donor. Employing the enzyme as electron donor enables a kinetically controlled supply of electrons to the LPMO. The rate of chitin oxidation by CBP21 is equal to that of cosubstrate (lactose) oxidation by cellobiose dehydrogenase, verifying the usage of two electrons in the LPMO catalytic mechanism. Lactose oxidation correlates directly with the rate of LPMO catalysis, a method for indirect determination of LPMO activity is implicated
physiological function
enzyme increases chitin solubilization yields of chitinases by up to 30fold and 20fold for alpha- and beta-chitin, respectively. The addition of LPMO10F leads to a substantial increase in the (GlcNAc)2:GlcNAc product ratio of chitinases, in reactions with alpha-chitin only
physiological function
in presence of lytic polysaccharide monooxygenase Cbp21, the apparent kcat values of chitinases ChiA and ChiB increase 6-9fold, while there is no effect on chitinase ChiC
physiological function
LPMO10 and a chitinase mutually enhance each others activities upon degrading chitin as the substrate
physiological function
presence of CBP21 increases solubilization of chitin substrates with high degrees of crystallinity when combined with each of the three chitinases ChiA, ChiB, or ChiC, but this synergy is reduced upon decline in crystallinity
physiological function
presence of LPMO10 increases the rate of chitin depolymerization by both chitinases ChiA and ChiB
physiological function
the full-length enzyme and the individual catalytic LPMO module boost the activity of an endochitinase equally well, also yielding similar amounts of oxidized products. When grown on insoluble chitin substrates, the deletion mutant shows a reproducible growth defect on beta-chitin leading to an 2fold slower growth rate compared with the wild type strain. When grown on crab shells, the mutation leads to an extended lag phase of about 100 h
physiological function
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presence of LPMO10 increases the rate of chitin depolymerization by both chitinases ChiA and ChiB
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physiological function
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cellobiose dehydrogenase from Myriococcum thermophilum can act as an electron donor. Employing the enzyme as electron donor enables a kinetically controlled supply of electrons to the LPMO. The rate of chitin oxidation by CBP21 is equal to that of cosubstrate (lactose) oxidation by cellobiose dehydrogenase, verifying the usage of two electrons in the LPMO catalytic mechanism. Lactose oxidation correlates directly with the rate of LPMO catalysis, a method for indirect determination of LPMO activity is implicated
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physiological function
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LPMO10 and a chitinase mutually enhance each others activities upon degrading chitin as the substrate
-
physiological function
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enzyme increases chitin solubilization yields of chitinases by up to 30fold and 20fold for alpha- and beta-chitin, respectively. The addition of LPMO10F leads to a substantial increase in the (GlcNAc)2:GlcNAc product ratio of chitinases, in reactions with alpha-chitin only
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