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Literature summary for 1.17.1.4 extracted from

  • Nguyen, J.; Feierabend, J.
    Some properties and subcellular localization of xanthine dehydrogenase in pea leaves (1978), Plant Sci. Lett., 13, 125-132.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
4-hydroxypyrazolo(3,4-d)pyrimidine 51% inhibition of hypoxanthine oxidation at 0.0001 mM Pisum sativum
KCN 63% inhibition at 1 mM Pisum sativum
Salicylhydroxamic acid 82% inhibition of hypoxanthine oxidation at 2.5 mM Pisum sativum

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol subcellular fractionation Pisum sativum 5829
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
hypoxanthine + NAD+ + H2O Pisum sativum
-
xanthine + NADH + H+
-
?
hypoxanthine + NADP+ + H2O Pisum sativum 40% of the activity compared to NAD+ xanthine + NADPH
-
?
xanthine + NAD+ + H2O Pisum sativum only present as stable dehydrogenase from, no conversion to the oxidase form urate + NADH
-
?
xanthine + O2 + H2O Pisum sativum low activity urate + O2- + 2 H+
-
?

Organism

Organism UniProt Comment Textmining
Pisum sativum
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Pisum sativum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hypoxanthine + methylene blue + H2O 39% of the activity compared to NAD+ as electron acceptor Pisum sativum xanthine + reduced methylene blue
-
?
hypoxanthine + NAD+ + H2O
-
Pisum sativum xanthine + NADH + H+
-
?
hypoxanthine + NADP+ + H2O 40% of the activity compared to NAD+ Pisum sativum xanthine + NADPH
-
?
hypoxanthine + phenazine methosulfate + H2O effective electron acceptor Pisum sativum urate + ?
-
?
xanthine + NAD+ + H2O only present as stable dehydrogenase from, no conversion to the oxidase form Pisum sativum urate + NADH
-
?
xanthine + O2 + H2O low activity Pisum sativum urate + O2- + 2 H+
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
-20
-
stable dehydrogenase form, no conversion to the oxidase form Pisum sativum
37
-
stable dehydrogenase activity, no conversion to the oxidase form Pisum sativum

Cofactor

Cofactor Comment Organism Structure
NAD+ cannot be replaced by NADP+ Pisum sativum
NADP+ 40% of the activity compared to NAD+ Pisum sativum