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首页> 外文期刊>Microbiology >An important role for glutathione and γ-glutamyltranspeptidase in the supply of growth requirements during nitrogen starvation of the yeast Saccharomyces cerevisiae
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An important role for glutathione and γ-glutamyltranspeptidase in the supply of growth requirements during nitrogen starvation of the yeast Saccharomyces cerevisiae

机译:谷胱甘肽和γ-谷氨酰胺转移酶在酵母糖酵母酿酒酵母的氮饥饿期间在生长要求供应中的重要作用

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摘要

When the yeast Saccharomyces cerevisiae Σ1278b was starved for nitrogen, the total glutathione (GSH) pool increased from 7 to 17 nmol (mg dry wt)-1 during the first 2 h and then declined. More than 90% of the total GSH shifted towards the central vacuole during this time. This transient stimulation was not observed in the presence of buthionine-(S,R)-sulphoximine (BSO), a specific transition-state-analogue inhibitor of γ-glutamylcysteine synthase (γ-GCS), nor in a mutant strain deficient in this enzyme. γ-Glutamyltranspeptidase (γ-GT), a vacuolar enzyme responsible for the initial step of GSH degradation, was derepressed during nitrogen starvation. This mechanism can apparently enable the starved yeast cell to use the constituent amino acids from GSH which accumulate in the vacuole to satisfy its growth requirements for nitrogen.
机译:当酵母酿酒酵母肠σ1278B终止氮气时,总谷胱甘肽(GSH)池在前2小时期间从7-17 nmol(Mg干燥重量)-1增加,然后下降。在此期间,超过90%的总GSH向中央液泡转移。在γ-谷氨酸氨基合酶(γ-GCS)的特定过渡 - 状态 - 类似物抑制剂(γ-GCS)的特定过渡 - 状态 - 类似物抑制剂中,未观察到这种瞬时刺激。(γ-GCS),也没有观察到γ-谷氨酸的特异性 - β-甲磺酰基合酶(γ-GCS),也不在缺乏突变菌株酶。 γ-谷氨酰胺转移酶(γ-GT),在氮饥饿期间对GSH降解初始步骤的初始步骤中的逼失酶。该机制显然能够使饥饿的酵母细胞能够使用来自GSH的组分氨基酸,该GSH积聚在液泡中以满足其对氮的生长要求。

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