QUINOLINATE PHOSPHORIBOSYL TRANSFERASE IS NOT THE OXYGEN-SENSITIVE SITE OF NICOTINAMIDE ADENINE-DINUCLEOTIDE BIOSYNTHESIS

被引：5

作者：

GARDNER, PR ^{[1
]}

FRIDOVICH, I ^{[1
]}

机构：

[1] DUKE UNIV,MED CTR,DEPT BIOCHEM,DURHAM,NC 27710

来源：

FREE RADICAL BIOLOGY AND MEDICINE | 1990年 / 8卷 / 02期

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

Free radicals; NAD[!sup]+[!/sup] biosynthesis-O[!sub]2[!/sub]-sensitive site; Oxygen toxicity; Quinolinate phosphoribosyl transferase;

D O I：

10.1016/0891-5849(90)90083-U

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Quinolinate phosphoribosyl transferase (QPT)1 activity was not affected when Escherichia coli were treated with hyperbaric oxygen. This result is not in accord with a previous report (Biochem. Biophys. Res. Comm. 91:982-990; 1979) in which the enzyme was shown to be rapidly inactivated in E. Coli exposed to 4.2 atmospheres of oxygen. Our data rule out QPT as a site of oxygen toxicity and suggest other mechanisms for the inhibitory effects of hyperbaric oxygen on pyridine nucleotide biosynthesis. © 1990.

引用

页码：117 / 119

页数：3

共 8 条

[1] Brown, Yein, Boehme, Foudin, Song, Oxygen poisoning of NAD biosynthesis: a proposed site of cellular oxygen toxicity, Biochem. Biophys. Res. Comm., 91, pp. 982-990, (1979)
[2] Brown, Song, Pyridine nucleotide coenzyme biosynthesis: a cellular site of oxygen toxicity, Biochem. Biophys. Res. Comm., 93, pp. 172-178, (1980)
[3] Heitkamp, Brown, Inhibition of NAD biosynthesis by paraquat in Escherichia coli, Biochim. Biophys. Acta, 676, pp. 345-349, (1981)
[4] Brown, Heitkamp, Song, Niacin reduces paraquat toxicity in rats, Science, 212, pp. 1510-1512, (1981)
[5] Lowry, Rosebrough, Farr, Randall, Protein measurement with the folin phenol reagent, J. Biol. Chem., 193, pp. 265-275, (1951)
[6] Packman, Jakoby, Quinolinate phosphoribosyl transferase, Biochem. Biophys. Res. Comm., 18, pp. 710-715, (1965)
[7] Nasu, Wicks, Gholson, L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase, J. Biol. Chem., 257, pp. 626-632, (1982)
[8] Flint, Emptage, Dihydroxy acid dehydratase—isolation, characterization as Fe-S proteins, and sensitivity to inactivation by oxygen radicals, Biosynthesis of branched chain amino acids, (1989)

← 1 →