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Literature summary for 1.7.1.10 extracted from

  • Trepanier, L.A.; Miller, J.L.
    NADH-dependent reduction of sulphamethoxazole hydroxylamine in dog and human liver microsomes (2000), Xenobiotica, 30, 1111-1121.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information not inhibited by a nitrogen atmosphere; not inhibited by azide, CO, dextromethorphan or erythromycin Canis lupus familiaris
additional information not inhibited by azide, CO, dextromethorphan or erythromycin Homo sapiens
N-Methylhydroxylamine
-
Canis lupus familiaris
N-Methylhydroxylamine
-
Homo sapiens
p-hydroxymercuribenzoate
-
Canis lupus familiaris
p-hydroxymercuribenzoate
-
Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
Homo sapiens
-
-
microsome
-
Canis lupus familiaris
-
-

Organism

Organism UniProt Comment Textmining
Canis lupus familiaris
-
2 enzyme forms are present, one may be identical to the multienzyme complex from pig
-
Homo sapiens
-
2 enzyme forms are present, one may be identical to the multienzyme complex from pig
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-
liver
-
Canis lupus familiaris
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sulphamethoxazole hydroxylamine + NADH + H+ activity in liver microsomes, NADH is preferred Homo sapiens sulphamethoxazole + NAD+ + H2O antimicrobial for the treatment of gastrointestinal, urinary and respiratory pathogens ?
sulphamethoxazole hydroxylamine + NADH + H+ activity in liver microsomes, NADH is preferred Canis lupus familiaris sulphamethoxazole + NAD+ + H2O antimicrobial for the treatment of gastrointestinal, urinary and respiratory pathogens ?

Cofactor

Cofactor Comment Organism Structure
NADH
-
Homo sapiens
NADH
-
Canis lupus familiaris