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：

美国国家科学基金会; 美国国家卫生研究院;

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

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[2]

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[3]

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[4]

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[7]

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[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)

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