Acyl phosphatase activity of NO-inhibited glyceraldehyde-3-phosphate dehydrogenase (GAPDH): a potential mechanism for uncoupling glycolysis from ATP generation in NO-producing cells
Acyl phosphatase activity of NO-inhibited glyceraldehyde-3-phosphate dehydrogenase (GAPDH): a potential mechanism for uncoupling glycolysis from ATP generation in NO-producing cells
复制标题
DOI：
10.1042/0264-6021:3410005
复制
发表时间：
1999-07-01
影响因子：
4.1
通讯作者：
Reichner, JS
中科院分区：
文献类型：
--
作者：
Albina, JE;Mastrofrancesco, B;Reichner, JS
在体外用NO供体S-亚硝基谷胱甘肽、3-吗啉代壬亚胺或二乙胺NONOate（diethylamine diazeniumdiolate）处理甘油醛-3-磷酸脱氢酶（GAPDH），可抑制其脱氢酶活性，诱导其酰基磷酸酶活性。反过来，NO产生细胞表现出GAPDH活性降低，糖酵解增加，ATP含量、合成和周转减少。这些细胞的变化可以解释为解偶联糖酵解通量从底物水平磷酸化的酰基磷酸酶活性NO修饰的GAPDH。
Treatment of glyceraldehyde-3-phosphate-dehydrogenase (GA(GAPDH) with the NO donors S-nitrosoglutathione, 3-morpholinusydnonimine or diethylamine NONOate (diethylamine diazeniumdiolate) in vitro, inhibited its dehydrogenase activity and induced its acyl phosphatase activity. NO-producing cells, in turn, exhibited reduced GAPDH activity, increased glycolysis, and decreased ATP content, synthesis and turnover. These cellular alterations could be explained by the uncoupling of glycolytic flux from substrate level phosphorylation by the acyl phosphatase activity of NO-modified GAPDH.