Literature DB >> 371772

Factors influencing the in vivo stability of L-serine deaminase activity in E. coli K12.

R D Beeraj, J F Morris, E B Newman.   

Abstract

L-Serine deaminase (L-SD) is unstable in intact cells of Escherichia coli K12. The extent of this instability is dependent on the nitrogen content of the medium in which the enzyme is synthesized, and on that in which it is tested. Enzyme activity in cells grown with an inorganic nitrogen source is unstable in the presence of inorganic nitrogen; enzyme activity in cells grown with an organic nitrogen source is unstable in the presence of the amino acids glycine and leucine.

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Year:  1978        PMID: 371772     DOI: 10.1139/m78-257

Source DB:  PubMed          Journal:  Can J Microbiol        ISSN: 0008-4166            Impact factor:   2.419


  1 in total

1.  L-Serine deaminase activity is induced by exposure of Escherichia coli K-12 to DNA-damaging agents.

Authors:  E B Newman; D Ahmad; C Walker
Journal:  J Bacteriol       Date:  1982-11       Impact factor: 3.490

  1 in total

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