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Literature summary for 1.14.99.53 extracted from

  • Zhang, H.; Zhao, Y.; Cao, H.; Mou, G.; Yin, H.
    Expression and characterization of a lytic polysaccharide monooxygenase from Bacillus thuringiensis (2015), Int. J. Biol. Macromol., 79, 72-75.
    View publication on PubMed
Search for more literature for 1.14.99.53

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 Bacillus thuringiensis
expression in Escherichia coli Bacillus thuringiensis serovar kurstaki

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ dependent on Bacillus thuringiensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
20000
-
-
 Bacillus thuringiensis serovar kurstaki
24150
-
 calculated from amino acid sequence Bacillus thuringiensis

Organism

Organism UniProt Comment Textmining
Bacillus thuringiensis A0A0C5K362 subsp. Kurstaki
-
Bacillus thuringiensis ACCC 10066 A0A0C5K362 subsp. Kurstaki
-
Bacillus thuringiensis serovar kurstaki A0A0C5K362
-
-
Bacillus thuringiensis serovar kurstaki ACCC 10066 A0A0C5K362
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus thuringiensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-chitin + ascorbate + O2
-
 Bacillus thuringiensis serovar kurstaki oxidized oligosaccharides + dehydroascorbate + H2O
-
 ?
alpha-chitin + ascorbate + O2
-
 Bacillus thuringiensis serovar kurstaki ACCC 10066 oxidized oligosaccharides + dehydroascorbate + H2O
-
 ?
beta-chitin + ascorbate + O2
-
 Bacillus thuringiensis serovar kurstaki oxidized oligosaccharides + dehydroascorbate + H2O
-
 ?
beta-chitin + ascorbate + O2
-
 Bacillus thuringiensis serovar kurstaki ACCC 10066 oxidized oligosaccharides + dehydroascorbate + H2O
-
 ?
chitin + acceptor + O2
-
 Bacillus thuringiensis [chitin oligosaccharide]-N-acetyl-D-glucosaminate + [chitin oligosaccharide]-N-acetyl-D-glucosamino-1,5-lactone the products are a series of chitin oligosaccharides in aldonic acid or lactone form with varying degree of polymerization: DPox4 > DPox5 > DPox6 > DPox7 > DPox8. Oligosaccharides with even-numbered chain lengths are predominant. ?
chitin + acceptor + O2
-
 Bacillus thuringiensis ACCC 10066 [chitin oligosaccharide]-N-acetyl-D-glucosaminate + [chitin oligosaccharide]-N-acetyl-D-glucosamino-1,5-lactone the products are a series of chitin oligosaccharides in aldonic acid or lactone form with varying degree of polymerization: DPox4 > DPox5 > DPox6 > DPox7 > DPox8. Oligosaccharides with even-numbered chain lengths are predominant. ?
colloidal chitin + ascorbate + O2
-
 Bacillus thuringiensis serovar kurstaki oxidized chitin oligosaccharides + dehydroascorbate + H2O with colloidal chitin as the substrate, a ladder of oxidized oligosaccharides is observed ?
colloidal chitin + ascorbate + O2
-
 Bacillus thuringiensis serovar kurstaki ACCC 10066 oxidized chitin oligosaccharides + dehydroascorbate + H2O with colloidal chitin as the substrate, a ladder of oxidized oligosaccharides is observed ?
crystalline chitin + ascorbate + O2
-
 Bacillus thuringiensis serovar kurstaki oxidized oligosaccharides + dehydroascorbate + H2O enzyme generates even-numbered oxidized oligosaccharides as the dominated products from crystalline chitin ?
crystalline chitin + ascorbate + O2
-
 Bacillus thuringiensis serovar kurstaki ACCC 10066 oxidized oligosaccharides + dehydroascorbate + H2O enzyme generates even-numbered oxidized oligosaccharides as the dominated products from crystalline chitin ?
additional information the enzyme produces oxidized chitin oligosaccharides with a degree of polymerization from DPox3 to DPox11. The relative intensities of DPox4, DPox6, DPox8 and DPox10 are remarkably higher than DPox5, DPox7, DPox9 and DPox11. LPMO10A shows little binding to Avicel Bacillus thuringiensis serovar kurstaki ?
-
 ?
additional information the enzyme produces oxidized chitin oligosaccharides with a degree of polymerization from DPox3 to DPox11. The relative intensities of DPox4, DPox6, DPox8 and DPox10 are remarkably higher than DPox5, DPox7, DPox9 and DPox11. LPMO10A shows little binding to Avicel Bacillus thuringiensis serovar kurstaki ACCC 10066 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 20000, SDS-PAGE, x * 20540, calculated Bacillus thuringiensis serovar kurstaki

Synonyms

Synonyms Comment Organism
AA10
-
 Bacillus thuringiensis serovar kurstaki
EF_0362
-
 Bacillus thuringiensis