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Literature summary for 1.14.99.53 extracted from

  • Kont, R.; Bissaro, B.; Eijsink, V.; Vaeljamaee, P.
    Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs) (2020), Nat. Commun., 11, 5786.
    View publication on PubMed
Search for more literature for 1.14.99.53

Application

Application Comment Organism
analysis method to kinetically assess the cellulolytic peroxygenase reaction using competition between well characterized reference enzymes and LPMOs for the H2O2 cosubstrate. LPMOs of both bacterial and fungal origin showed high peroxygenase efficiencies, with kcat/KmH2O2 values in the order of 100-1000 mM/s Serratia marcescens
analysis method to kinetically assess the cellulolytic peroxygenase reaction using competition between well characterized reference enzymes and LPMOs for the H2O2 cosubstrate. LPMOs of both bacterial and fungal origin showed high peroxygenase efficiencies, with kcat/KmH2O2 values in the order of 100-1000 mM/s Streptomyces coelicolor

Organism

Organism UniProt Comment Textmining
Serratia marcescens
-
-
-
Streptomyces coelicolor
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cellulose + ascorbate + O2
-
 Streptomyces coelicolor ? + dehydroascorbate + H2O
-
 ?
chitin + ascorbate + O2
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 Serratia marcescens C1-oxidized chito-oligosaccharides + dehydroascorbate + H2O
-
 ?
additional information enzyme additionally shows peroxigenase activity. The peroxygenase reaction is faster than the monooxygenase reaction Serratia marcescens ?
-
 ?
additional information enzyme additionally shows peroxigenase activity. The peroxygenase reaction is faster than the monooxygenase reaction Streptomyces coelicolor ?
-
 ?

Synonyms

Synonyms Comment Organism
AA10A
-
 Serratia marcescens
AA10C
-
 Streptomyces coelicolor
CelS2
-
 Streptomyces coelicolor