Role of L-threonine dehydrogenase in the catabolism of threonine and synthesis of glycine by Escherichia coli.
The enzyme L-threonine dehydrogenase was demonstrated in extracts of Escherichia coli K-12, and was shown to be the first enzyme of the pathway converting threonine to glycine. The enzyme was induced by L-leucine, but not by its substrate, L-threonine. The metabolic significance of leucine as a catabolic signal for amino acid degradation is considered.
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D002474:Cell-Free System; D004790:Enzyme Induction; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism*; D005998:Glycine / Q000096:biosynthesis* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007930:Leucine / Q000378:metabolism; D009154:Mutation; D013237:Stereoisomerism; D013912:Threonine / Q000378:metabolism*
D013912:Threonine; D000429:Alcohol Oxidoreductases; D007930:Leucine; D005998:Glycine