The catabolism of L-tyrosine by an Arthrobacter sp.

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Abstract
An Arthrobacter sp. metabolizes L-tyrosine by a pathway involving 3,4-dihydroxyphenylacetate as a key intermediate. p-Hydroxyphenylpyruvate is formed from tyrosine by an aminotransferase specifically requiring .alpha.-ketoglutarate for activity, and is then converted to p-hydroxyphenylacetate by an oxidative decarboxylation. p-Hydroxyphenylacetaldehyde is not an intermediate in the formation of p-hydroxyphenylacetate. Extracts of the bacterium oxidize 3,4-dihydroxyphenylacetate to .delta.-carboxymethyl-.alpha.-hydroxymuconic acid which, when supplemented with 2 mol of diphosphopyridine dinucleotide, results in the production of stoichiometric amounts of succinate and pyruvate.