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- W2016348503 abstract "Larval tobacco budworm, Heliothis virescens [Noctuidae]are aggressive, generalist feeders that tolerate high levels of dietary l-canavanine, an insecticidal l-arginine antimetabolite; the LC50 for dietary canavanine is 300 mM. Arginine kinase (adenosine 5′ triphosphate: l-arginine phosphotransferase, EC 3.5.3.1), which mediates a phosphorylation of canavanine to yield the novel phosphagen, L-canavanine phosphate, was purified from larval gut. Kinetic parameters revealed an apparent Km value of 7.2 × 10−4 and 2.13 × 10−2M for arginine and canavanine, respectively. These Km values suggest that arginine kinase's affinity for canavanine is substantially less than its affinity for arginine. The ability of arginine kinase to metabolize canavanine accounts for the enhancement in canavanine catabolism in the presence of ATP observed in canavanine-treated larvae. Canavanine is a more effective substrate for arginine kinase than homoarginine, 2-amino-4-guanidinobutyric acid, and 2-amino-3-guanidinopropionic acid. However, all the arginine analogs were more active substrates for arginine kinase than homocanavanine and 2-amino-3-guanidinooxypropionic acid, the higher and lower canavanine analogs, respectively. When arginine kinase reacted with N-tris[hydroxymethyllmethylglycine (tricine) massive amounts of an unidentified, but ninhydrin-positive product was formed. The larvae showed no detectable loss in their ability to deal with dietary canavanine in the presence of tricine buffer." @default.
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- W2016348503 date "1995-09-01" @default.
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- W2016348503 title "Purification of l-arginine kinase from the tobacco budworm, Heliothis virescens [Noctuidae] and its function in l-canavanine detoxification" @default.
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- W2016348503 doi "https://doi.org/10.1016/0965-1748(95)00034-s" @default.
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