Novel quinolinequinone antitumor agents: structure-metabolism studies with NAD(P)H:quinone oxidoreductase (NQO1).
The effects of functional group changes on the metabolism of novel quinolinequinones by recombinant human NAD(P)H:quinone oxidoreductase (NQO1) are described. Overall, the quinolinequinones were much better substrates for NQO1 than analogous indolequinones, with compounds containing heterocyclic substituents at C-2 being among the best substrates.
Fryatt
T
T
School of Chemistry, University of Exeter, Devon, UK.
Goroski
D T
DT
Nilson
Z D
ZD
Moody
C J
CJ
Beall
H D
HD
D000970:Antineoplastic Agents / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D006801:Humans; D009247:NADH, NADPH Oxidoreductases / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*; D015363:Quinolones / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D011994:Recombinant Proteins / Q000187:drug effects / Q000378:metabolism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D000970:Antineoplastic Agents; D015363:Quinolones; D011994:Recombinant Proteins; D009247:NADH, NADPH Oxidoreductases