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Biomedical subjects

E B Newman

Publications and source records attributed to E B Newman.

49 records · Page 3Linked to original sources
PubMed1977

Role of threonine dehydrogenase in Escherichia coli threonine degradation.

Threonine was used as nitrogen source by Escherichia coli K-12 through a pathway beginning with the enzyme threonine dehydrogenase. The 2-amino-3-ketobutyrate formed was converted to glycine, and the glycine was converted to serine, which acted as the actual nitrogen donor. The enzyme formed under anaerobic conditions and known as threonine deaminase (biodegradative) is less widespread than threonine dehydrogenase and may be involved in energy metabolism rather than in threonine degradation per se.

Adenylyl Cyclases↗
PubMed1976

The conversion of leucine to alpha-ketoisocaproic acid and its metabolic consequences for Escherichia coli K12.

The amino acid L-leucine serves as a good auxiliary nitrogen source for Escherichia coli K12, and in so doing is converted to alpha-ketoisocaproic acid which is excreted into the medium. L-Leucine does not serve as sole nitrogen source. Cells incubated with L-leucine as sole nitrogen source do not grow, although they do metabolize leucine, and accumulate ketoisocaproic acid in the medium. Where glycine is the only other nitrogen source, the presence of L-leucine greatly increases the growth rate even at concentrations so low that its contribution as nitrogen donor is unlikely to be important.

Ammonium Sulfate↗
PubMed1975

Derivation of glycine from threonine in Escherichia coli K-12 mutants.

Escherichia coli AT2046 has been shown previously to lack the enzyme serine transhydroxymethylase and to require exogenous glycine for growth as a consequence. Strains JEV73 and JEV73R, mutants derived from strain AT2046, are shown here to be serine transhydroxymethylase deficient, but able to derive their glycine from endogenously synthesized threonine. Leucine is shown to be closely involved in the regulation of biosynthesis of glycine, to spare glycine in strain AT2046T, to replace glycine in strain JEV73, and to increase threonine conversion to glycine in a representative prototroph of E. coli. An interpretation of strains JEV73 and JEV73R as regulatory mutants of strain AT2046 is given. A hypothesis as to the role of leucine as a signal for nitrogen scavenging is suggested.

Aspartic Acid↗
PubMed1974

Studies on L-serine deaminase in Escherichia coli K-12.

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.

Amino Acids↗