Literature summary for 1.17.1.4 extracted from

Asai, R.; Nishino, T.; Matsumura, T.; Okamoto, K.; Igarashi, K.; Pai, E.F.; Nishino, T.
Two mutations convert mammalian xanthine oxidoreductase to highly superoxide-productive xanthine oxidase (2007), J. Biochem., 141, 525-534.

Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant W335A/F336L, showing two similar, but not identical subunits. The cluster involved in conformation-switching is completely disrupted in one subunit, but remains partly associated in the other. Xanthine oxidase and oxidoreductase forms of the mutant are in equilibrium that greatly favors the oxidase form, but upon incubation with dithiothreitol equilibrium is partly shifted towards the oxidoreductase form	Rattus norvegicus

Crystallization (Comment)

Organism

mutant W335A/F336L, showing two similar, but not identical subunits. The cluster involved in conformation-switching is completely disrupted in one subunit, but remains partly associated in the other. Xanthine oxidase and oxidoreductase forms of the mutant are in equilibrium that greatly favors the oxidase form, but upon incubation with dithiothreitol equilibrium is partly shifted towards the oxidoreductase form

Rattus norvegicus

Protein Variants

Protein Variants	Comment	Organism
W335A/F336L	mutant oxidoreductase displaying xanthine oxidase activity	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	P22985	conversion of oxidoreductatse to oxidase	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
xanthine + NAD+ + H2O	-	Rattus norvegicus	urate + NADH + H+	-	?

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Release 2023.1 (January 2023)