Studies on l-Serine Deaminase in Escherichia coli K-12
AUTOR(ES)
Isenberg, S.
RESUMO
l-Serine deaminase has been studied in toluene-treated cells of Escherichia coli K-12 and shown to be a discrete entity distinct from l-threonine deaminase. Its level in the cell varies as a function of nitrogen nutrition, carbon source, and amino acids (glycine and leucine). The metabolic role of the enzyme remains unclear but may be related to serine toxicity. The enzyme is unstable within the cell in the presence of its inducers, glycine and leucine, but not in their absence.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=246639Documentos Relacionados
- A novel L-serine deaminase activity in Escherichia coli K-12.
- l-Serine Deaminase of Escherichia coli
- L-Serine deaminase activity is induced by exposure of Escherichia coli K-12 to DNA-damaging agents.
- In vitro and in vivo activation of L-serine deaminase in Escherichia coli K-12.
- A mutation in Escherichia coli K-12 results in a requirement for thiamine and a decrease in L-serine deaminase activity.
