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Literature summary for 1.17.3.2 extracted from

  • Waud, W.R.; Rajagopalan, K.V.
    Purification and properties of the NAD+-dependent (type D) and O2-dependent (type O) forms of rat liver xanthine dehydrogenase (1976), Arch. Biochem. Biophys., 172, 354-364.
    View publication on PubMed
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General Stability

General Stability Organism
rat liver enzyme is unstable as dehydrogenase and is gradually converted to oxidase Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.002
-
 xanthine
-
 Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Iron iron-molybdenum protein Rattus norvegicus
Molybdenum an iron-molybdenum protein Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information liver enzyme is unstable as dehydrogenase and is gradually converted to oxidase Rattus norvegicus
proteolytic modification
-
 Rattus norvegicus

Purification (Commentary)

Purification (Comment) Organism
-
 Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hypoxanthine + 2 H2O + 2 O2
-
 Rattus norvegicus urate + 2 H2O2
-
 ?
xanthine + H2O + O2 electron acceptor O2 Rattus norvegicus uric acid + H2O2
-
 ?

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein Rattus norvegicus