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Literature summary extracted from

  • Loose, J.S.; Forsberg, Z.; Kracher, D.; Scheiblbrandner, S.; Ludwig, R.; Eijsink, V.G.; Vaaje-Kolstad, G.
    Activation of bacterial lytic polysaccharide monooxygenases with cellobiose dehydrogenase (2016), Protein Sci., 25, 2175-2186.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.99.53 expression in Escherichia coli Streptomyces coelicolor

Organism

EC Number Organism UniProt Comment Textmining
1.14.99.53 Streptomyces coelicolor V5N5H9
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-
1.14.99.53 Streptomyces coelicolor ATCC BAA-471 V5N5H9
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.99.53 beta-chitin + ascorbate + O2
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 Streptomyces coelicolor C1-oxidized oligosaccharides + dehydroascorbate + H2O
-
 ?
1.14.99.53 beta-chitin + ascorbate + O2
-
 Streptomyces coelicolor ATCC BAA-471 C1-oxidized oligosaccharides + dehydroascorbate + H2O
-
 ?
1.14.99.53 beta-chitin + cellobiose dehydrogenase + O2 cellobiose dehydrogenase from Myriococcum thermophilum can act as an electron donor Streptomyces coelicolor C1-oxidized oligosaccharides + reduced cellobiose dehydrogenase + H2O
-
 ?
1.14.99.53 beta-chitin + cellobiose dehydrogenase + O2 cellobiose dehydrogenase from Myriococcum thermophilum can act as an electron donor Streptomyces coelicolor ATCC BAA-471 C1-oxidized oligosaccharides + reduced cellobiose dehydrogenase + H2O
-
 ?
1.14.99.53 additional information enzyme in presence of ascorbate but lacking chitin produces H2O2 Streptomyces coelicolor ?
-
 ?
1.14.99.53 additional information enzyme in presence of ascorbate but lacking chitin produces H2O2 Streptomyces coelicolor ATCC BAA-471 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.99.53 CelS2
-
 Streptomyces coelicolor

General Information

EC Number General Information Comment Organism
1.14.99.53 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 Streptomyces coelicolor