Reversible inactivation of isocitrate dehydrogenase in Escherichia coli.
نویسندگان
چکیده
Escherichia coli can grow aerobically in defined media containing inorganic salts and any one of a wide range of carbon compounds. Whatever the nature of the carbon source. it is fed into the amphibolic pathways [glycolysis, pentose phosphate pathway, Krebs (tricarboxylic acid) cyclel, from which stem all the biosynthetic pathways required for making the components of new cell material. The operation of the amphibolic pathways also traps energy in the forms (ATP, NADPH, H+) required for biosynthesis and growth. These processes are common to growth on any carbon source, but biosynthesis also relies on anaplerotic sequences of metabolism which replenish the pools of some compounds (e.g. in the Krebs cycle) which are the starting points for biosynthesis (Kornberg. 1966). Different anaplerotic sequences are used according to the point at which any particular carbon source enters the amphibolic pathways. For example, growth on glucose (Fig. 1) depends on the
منابع مشابه
Regulation of isocitrate dehydrogenase by phosphorylation in Escherichia coli K-12 and a simple method for determining the amount of inactive phosphoenzyme.
In several Escherichia coli K-12 strains grown on a limiting concentration of glucose, isocitrate dehydrogenase (IDH) was inactivated about 90% after cessation of growth upon exhaustion of the glucose. Such inactivation has been previously observed in several E. coli strains but not in E. coli K-12 (unless acetate was added to the bacterial culture when growth ceased). IDH was inactivated 75 to...
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The regulation of enzyme activity by reversible covalent phosphorylation has been reviewed by Krebs & Beavo (1979). Although this mechanism of modulating the catalytic activity of enzymes is well known in many eukaryotic systems, it has been reported only recently in bacteria. At this time, NADP:isocitrate dehydrogenase (EC 1.1.1.42) is the only one of several phosphorylated bacterial proteins ...
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ورودعنوان ژورنال:
- Biochemical Society transactions
دوره 10 5 شماره
صفحات -
تاریخ انتشار 1982