Limited proteolysis of glutamine synthetase is inhibited by glutamate and by feedback inhibitors.
نویسندگان
چکیده
منابع مشابه
Regulation of glutamine synthetase from Bacillus subtilis by divalent cations, feedback inhibitors, and L-glutamine.
Glutamine synthetase purified to apparent homogeneity from Bacillus subtilis is subject to feedback inhibition by multiple end products of glutamine metabolism, as well as by the reaction product L-glutamine. AMP, glutamine, and histidine are potent inhibitors when any of the substrates glutamate, MnATP, or ammonia are present in limiting concentration during assay, but the strong inhibition by...
متن کاملRegulation of synthesis of glutamine synthetase by adenylylated glutamine synthetase.
We have examined three mutants of Klebsiella aerogenes whose genetic lesions (glnB, glnD, and glnE) are in loci unlinked to the structural gene for glutamine sythetase (glnA) and in which the control of both the level and state of adenylylation of glutamine synthetase is altered. Each mutation alters a different component of the adenylylation system of glutamine synthetase [L-glutamate:ammonia ...
متن کاملChloroplastic glutamine synthetase is activated by direct binding of aluminium.
Acidification of soils may release water soluble, toxic aluminium species from clay minerals. Al interferes with a wide range of physical and cellular processes. Glutamine synthetase (GS, EC 6.3.1.2) is the key enzyme of primary N assimilation, as well as ammonia reassimilation and detoxification. Plant GS requires two magnesium ions per subunit for activity, which makes GS a potential target o...
متن کاملProbing Conformational Feature of a Recombinant Pyruvate Kinase by Limited Proteolysis
Pyruvate kinase is a key enzyme in glycolytic pathway that catalyzes the transphosphorylation between phosphoenolpyruvate and ADP to yield ATP and Pyruvate. Geobacillus stearothermophillus has a stable pyruvate kinase with determined crystal structure that composed of four separate domains. Given that limited proteolysis experiments can be successfully used to probe conformational features of p...
متن کاملTurnover of bacterial glutamine synthetase: oxidative inactivation precedes proteolysis.
We partially purified a preparation from Escherichia coli that proteolytically degrades the enzyme glutamine synthetase [L-glutamate:ammonia ligase (ADP-forming), EC 6.3.1.2]. The degradation is at least a two-step process. First, the glutamine synthetase undergoes an oxidative modification. This modification leads to loss of catalytic activity and also renders the protein susceptible to proteo...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1979
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)30192-8