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Literature summary for 1.6.5.5 extracted from

  • Alharbi, I.; Khan, M.; Rabbani, N.; Al-Senaidy, A.; Ismael, M.; Ayoub, M.
    Inhibition of NADPH quinone oxidoreductase activity of camel lens zeta-crystallin by colchicine (2014), Curr. Enzyme Inhib., 10, 137-142 .
No PubMed abstract available
Search for more literature for 1.6.5.5

Inhibitors

Inhibitors Comment Organism Structure
Colchicine noncompetitive with respect to 9,10-phenanthrenequinone and 1,2-naphthoquinone, uncompetitive with respect to NADPH. Binding of colchicine occurs at or close to the NADPH binding site Camelus sp.

Organism

Organism UniProt Comment Textmining
Camelus sp.
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
lens
-
 Camelus sp.
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 1,2-naphthoquinone + NADPH + H+
-
 Camelus sp. 2 1,2-naphthosemiquinone + NADP+
-
 ?
2 9,10-phenanthrenequinone + NADPH + H+
-
 Camelus sp. 2 9,10-phenanthrenesemiquinone + NADP+
-
 ?

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0015
-
 pH not specified in the publication, temperature not specified in the publication Camelus sp. Colchicine