Factors influencing the in vivo stability of L-serine deaminase activity in E. coli K12.
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.
D000645:Ammonium Sulfate / Q000378:metabolism; D003470:Culture Media; D004790:Enzyme Induction; D004926:Escherichia coli / Q000201:enzymology*; D005947:Glucose / Q000378:metabolism; D005998:Glycine / Q000378:metabolism; D007532:Isoleucine / Q000378:metabolism; D012695:L-Serine Dehydratase / Q000378:metabolism*; D007930:Leucine / Q000378:metabolism; D010088:Oxidoreductases / Q000378:metabolism; D013913:Threonine Dehydratase / Q000378:metabolism
D003470:Culture Media; D007532:Isoleucine; D010088:Oxidoreductases; D012695:L-Serine Dehydratase; D013913:Threonine Dehydratase; D007930:Leucine; D005947:Glucose; D000645:Ammonium Sulfate; D005998:Glycine