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Literature summary for 1.17.1.4 extracted from

  • Yen, T.T.T.; Glassman, E.
    Electrophoretic variants of xanthine dehydrogenase in Drosophila melanogaster: II. Enzyme kinetics (1967), Biochim. Biophys. Acta, 146, 35-44.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2-amino-4-hydroxypteridine-6-carboxyaldehyde competitive inhibition of 2-amino-4-hydoxy-pterine oxidation, Ki: 0.000016 mM Bos taurus
2-amino-4-hydroxypteridine-6-carboxyaldehyde competitive inhibition of 2-amino-4-hydroxy-pterine oxidation, Ki: 0.00025 mM, non-competitive inhibition of xanthine oxidation, Ki: 0.00051 mM Drosophila melanogaster
8-Azaguanine competitive inhibition of 2-amino-4-hydroxypterine oxidation, Ki: 0.0012 mM Bos taurus
8-Azaguanine competitive inhibition of xanthine oxidation, Ki: 0.037 mM, non-competitive inhibition of 2-amino-4-hydroxy-pterine oxidation, Ki: 0.071 mM Drosophila melanogaster
ammeline competitive inhibition of 2-amino-4-hydroxy-pterine oxidation, Ki: 0.016 mM Bos taurus
ammeline competitive inhibition of xanthine oxidation, Ki: 0.021 mM, non-competitive inhibition of 2-amino-4-hydoxypterine oxidation, Ki: 0.045 mM Drosophila melanogaster
pyridoxal Ki for 2-amino-4-hydroxypterine oxidation: 0.08 mM at 30 and 50°C, competitive; Ki for xanthine oxidation: 0.05 mM at 30°C, 0.11 mM at 50°C, competitive Drosophila melanogaster
xanthine substrate inhibition above 0.05 mM, but in the presence of NAD+ Drosophila melanogaster

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00083
-
methylene blue electron donor: 2-amino-4-hydroxy-pterine Drosophila melanogaster
0.001
-
2-amino-4-hydroxypterin
-
Bos taurus
0.0033
-
NAD+ electron donor: 2-amino-4-hydroxypterine Drosophila melanogaster
0.004
-
2-amino-4-hydroxypterin pH 7.0, electron acceptor: methylene blue Drosophila melanogaster
0.0071
-
2-amino-4-hydroxypterin pH 8.0, electron acceptor: methylene blue Drosophila melanogaster
0.011
-
2-amino-4-hydroxypterin increased Km in the presence of pyridoxal Drosophila melanogaster
0.018
-
xanthine electron acceptor: NAD+, 30°C Drosophila melanogaster
0.025
-
NAD+ electron donor: xanthine Drosophila melanogaster
0.036
-
xanthine increased Km in the presence of pyridoxal at 30°C Drosophila melanogaster
0.04
-
xanthine electron acceptor: NAD+, 50°C Drosophila melanogaster
0.059
-
xanthine increased Km in the presence of pyridoxal at 50°C Drosophila melanogaster

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-amino-4-hydroxy-pterin + NAD+ + H2O Drosophila melanogaster i.e. pterin isoxanthopterin + NADH
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O Bos taurus i.e. pterin isoxanthopterin + NADH
-
?
xanthine + NAD+ + H2O Drosophila melanogaster
-
urate + NADH
-
?
xanthine + NAD+ + H2O Bos taurus
-
urate + NADH
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Drosophila melanogaster
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
milk
-
Bos taurus
-
whole body five different forms in electrophoretic mobility, but no differences in kinetic constants Drosophila melanogaster
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-amino-4-hydroxy-pterin + methylene blue + H2O
-
Drosophila melanogaster isoxanthopterin + reduced methylene blue
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O i.e. pterin Drosophila melanogaster isoxanthopterin + NADH
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O i.e. pterin Bos taurus isoxanthopterin + NADH
-
?
2-amino-4-hydroxypterin + NAD+ + H2O i.e. pterin Drosophila melanogaster isoxanthopterin + NADH
-
?
2-amino-4-hydroxypterin + NAD+ + H2O i.e. pterin Bos taurus isoxanthopterin + NADH
-
?
xanthine + NAD+ + H2O
-
Drosophila melanogaster urate + NADH
-
?
xanthine + NAD+ + H2O
-
Bos taurus urate + NADH
-
?

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Drosophila melanogaster
NAD+
-
Bos taurus