Literature summary for 1.17.1.4 extracted from

Enroth, C.; Eger, B.T.; Okamoto, K.; Nishino, T.; Nishino, T.; Pai, E.F.
Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion (2000), Proc. Natl. Acad. Sci. USA, 97, 10723-10728.

Search for more literature for 1.17.1.4

Activating Compound

Activating Compound	Comment	Organism	Structure
thiol active compounds	reversible conversion of xanthine dehydrogenase to xanthine oxidase by modification of C535 and C992 and formation of a disulfide bond, that induces a conformational change	Bos taurus

Crystallization (Commentary)

Crystallization (Comment)	Organism
2.1 A resolution for both xanthine oxidase and dehydrogenase forms, irreversible pancreatin cleaved xanthine oxidase form results in blocking access of substrate NAD+ to the FAD cofactor	Bos taurus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron-sulfur-center	2 Fe2-S2-clusters, located at the N-terminal 20 kDa domain	Bos taurus
molybdenum-center	C-terminal 85 kDa molybdopterin-binding domain	Bos taurus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
145000	-	2 * 145000, data from crystallization	Bos taurus
290000	-	-	Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
hypoxanthine + NAD+ + H2O	Bos taurus	-	xanthine + NADH + H+	-	?
xanthine + NAD+ + H2O	Bos taurus	-	urate + NADH	-	?

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Bos taurus

Source Tissue

Source Tissue	Comment	Organism	Textmining
milk	-	Bos taurus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
hypoxanthine + NAD+ + H2O	-	Bos taurus	xanthine + NADH + H+	-	?
xanthine + NAD+ + H2O	-	Bos taurus	urate + NADH	-	?

Subunits

Subunits	Comment	Organism
dimer	2 * 145000, data from crystallization	Bos taurus

Cofactor

Cofactor	Comment	Organism	Structure
FAD	one FAD per subunit, central 40 kDa FAD-domain	Bos taurus
additional information	-	Bos taurus
NAD+	-	Bos taurus

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Release 2023.1 (January 2023)