Literature summary extracted from

Loo, T.L.; Lim, C.; Johns, D.G.
Enzymic hydroxylation of 6-methylthiopurine by hepatic aldehyde oxidase (1967), Biochim. Biophys. Acta, 134, 467-469.

No PubMed abstract available

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
1.2.3.1	menadione	-	Oryctolagus cuniculus

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.2.3.1	0.2	-	6-methylthiopurine	O2 as electron acceptor	Oryctolagus cuniculus
1.2.3.1	0.3	-	6-methylthiopurine	2,6-dichlorophenol indophenol as electron acceptor	Oryctolagus cuniculus

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.2.3.1	Oryctolagus cuniculus	-	-	-

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
1.2.3.1	liver	-	Oryctolagus cuniculus	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.2.3.1	6-methylthiopurine + H2O + O2	2,6-dichlorophenol indophenol can also act as electron acceptor	Oryctolagus cuniculus	6-methylthio-8-hydroxypurine + H2O2	-	?

Ki Value [mM]

EC Number	Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
1.2.3.1	0.005	-	menadione	-	Oryctolagus cuniculus

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Release 2023.1 (January 2023)