Abstract
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.
MeSH terms
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Alcohol Oxidoreductases / metabolism*
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Cell-Free System
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Enzyme Induction
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Escherichia coli / enzymology
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Escherichia coli / metabolism*
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Glycine / biosynthesis*
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Glycine / metabolism
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Hydrogen-Ion Concentration
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Leucine / metabolism
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Mutation
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Stereoisomerism
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Threonine / metabolism*
Substances
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Threonine
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Alcohol Oxidoreductases
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Leucine
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Glycine