Literature summary for 1.10.3.3 extracted from

Murata, K.; Nakamura, N.; Ohno, H.
Elucidation of the factors affecting the oxidative activity of Acremonium sp. HI-25 ascorbate oxidase by an electrochemical approach (2008), Biochem. Biophys. Res. Commun., 367, 457-461.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
copper	the oxidative activity of ascorbate oxidase is dominated by the highly selective substrate-binding affinity based on electrostatic interaction beyond the one-electron redox potential difference between type 1 copper site of ascorbate oxidase and substrate	Acremonium sp.

Organism

Organism	UniProt	Comment	Textmining
Acremonium sp.	-	HI-25	-
Acremonium sp. HI-25	-	HI-25	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the oxidative activity of ascorbate oxidase is dominated by the highly selective substrate-binding affinity based on electrostatic interaction beyond the one-electron redox potential difference between type 1 copper site of ascorbate oxidase and substrate	Acremonium sp.	?	-	?
additional information	the oxidative activity of ascorbate oxidase is dominated by the highly selective substrate-binding affinity based on electrostatic interaction beyond the one-electron redox potential difference between type 1 copper site of ascorbate oxidase and substrate	Acremonium sp. HI-25	?	-	?

Synonyms

Synonyms	Comment	Organism
ASOM	-	Acremonium sp.

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Release 2023.1 (January 2023)