Subunit interaction in unadenylylated glutamine synthetase from Escherichia coli. Evidence from methionine sulfoximine inhibition studies.
نویسندگان
چکیده
منابع مشابه
Conformational differences between unadenylylated and adenylylated glutamine synthetase from Escherichia coli on binding L-methionine sulfoximine.
متن کامل
Studies on glutamine synthetase from Escherichia coli. Formation of pyrrolidone carboxylate and inhibition by methionine sulfoximine.
Both the adenylylated and unadenylylated forms of Escherichia coli glutamine synthetase catalyze the formation of pyrrolidone carboxylate from glutamate in the presence of ATP and divalent metal ions (Mg++ or Mn++) and in the absence of ammonia. The unadenylylated enzyme catalyzes this reaction more rapidly with Mg++ than with Mn++, while the adenylylated enzyme catalyzes it more rapidly with M...
متن کاملInhibition of glutamine synthetase by methionine sulfoximine. Studies on methionine sulfoximine phosphate.
The irreversible inhibition of glutamine synthetase by methionine sulfoximine is associated with the tight binding to the enzyme of adenosine diphosphate and methionine sulfoximine phosphate; the latter compound can be cleaved nonenzymatically and also by phosphatases to equimolar amounts of methionine sulfoximine and inorganic phosphate. Methionine sulfoximine phosphate is oxidized by L-amino ...
متن کاملStudies on Glutamine Synthetase from Escherichia coli FORMATION OF PYRROLIDONE CARBOXYLATE AND INHIBITION BY METHIONINE
Both the adenylylated and unadenylylated forms of Escherichia coli glutamine synthetase catalyze the formation of pyrrolidone carboxylate from glutamate in the presence of ATP and divalent metal ions (Mg++ or Mn++) and in the absence of ammonia. The unadenylylated enzyme catalyzes this reaction more rapidly with Mg++ than with Mn++, while the adenylylated enzyme catalyzes it more rapidly with M...
متن کاملL-Methionine SR-sulfoximine-resistant glutamine synthetase from mutants of Salmonella typhimurium.
Two mutants of Salmonella typhimurium resistant to growth inhibition by the glutamine synthetase transition state analog, L-methionine SR-sulfoximine, were isolated and characterized. These mutants are glutamine bradytrophs and cannot use growth rate-limiting nitrogen sources. Although this phenotype resembles that of mutants with lesions in the regulatory gene for glutamine synthetase, glnG, t...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1981
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)70022-2