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Literature summary for 1.4.3.14 extracted from

  • Guerrieri, A.; Ciriello, R.; Bianco, G.; De Gennaro, F.; Frascaro, S.
    Allosteric enzyme-based biosensors-kinetic behaviours of immobilised L-lysine-alpha-oxidase from Trichoderma viride pH influence and allosteric properties (2020), Biosensors, 10, 145 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
analysis L-lysine-alpha-oxidase is immobilised by co-crosslinking onto the surface of a Pt electrode. The resulting amperometric biosensor is able to analyse L-lysine. The immobilised enzymes and amperometric biosensor can be used for substrate analysis and as a convenient tool for enzyme kinetic studies Trichoderma viride

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lysine + O2 + H2O Trichoderma viride
-
6-amino-2-oxohexanoate + NH3 + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Trichoderma viride
-
i.e. Trichoderma viride
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine + O2 + H2O
-
Trichoderma viride 6-amino-2-oxohexanoate + NH3 + H2O2
-
?

Synonyms

Synonyms Comment Organism
L-lysine-alpha-oxidase
-
Trichoderma viride