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S-adenosylmethionine synthetase in methionine regulatory mutants of Salmonella typhimurium

โœ Scribed by Hobson, Ann C. ;Smith, D. A.


Publisher
Springer
Year
1973
Tongue
English
Weight
782 KB
Volume
126
Category
Article
ISSN
0026-8925

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Some metK mutants of Salmonella typhimurium with constitutive methionine biosynthesis have no detectable S-adenosylmethionine (SAM) synthetase, the enzyme which converts methionine to SAM, the postulated corepressor of the methionine pathway. However, these mutants are not auxotrophic for SAM, an es

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A defect in the repression of the de novo purine biosynthetic enzymes was detected among purA mutants of Salmonella typhimurium. We suggest that the defect is caused by an altered purine regulation gene (purR) which affects the response level of at least five of the de novo enzymes to repression by