The Journal of Biological Cheyistry
نویسنده
چکیده
In 1956, McDaniel, Hundley, and Sebrell (1) reported that urinary excretion of N’n~ethylnicotinamide decreased in alloxan-diabetic rats. Mehler, McDaniel, and Hundley (2) subsequently showed that the level of liver picolinic carboxylase increased markedly in alloxan-diabetic rats and was inversely related with urinary excretion of N’-methylnicotinamide. Previous nutritional studies have indicated that capacity of converting tryptophan to niacin varies with species of animals (3, 4). Cats apparently cannot utilize tryptophan in place of niacin (5). Suhadolnik et al. (6) reported that picolinic carboxylase activity in the cat liver is much higher than that in the rat liver. Recent reports from our laboratory described two metabolic pathways of tryptophan metabolism in mammals diverging from 3-hydroxyanthranilate: a biosynthetic pathway of nicotinamide adenine dinucleotide from 3-hydroxyanthranilate (referred to hereafter as the NA D pathzcag) (7,8) and a complete degradativc pathway of the benzene ring of tryptophan via glutaryl-Coil (the glutarate pathuay) (9-12) (Scheme 1). This paper describes the exljerimental evidence indicating that the biosynthesis of iYAD from tryptophan is controlled, at least in part, by picolinic carboxylase; this evidence explains the difference in the nutritional requirement of niacin between the cat and other mammals as well as the decrease in N’-methylnicotinamide excreted in the urine of alloxan-diabetic rats.
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تاریخ انتشار 2003