Abstract
An Arthrobacter sp. metabolizes L-tyrosine by a pathway involving 3,4-dihydroxyphenyl-acetate as a key intermediate. p-Hydroxyphenylpyruvate is formed from tyrosine by an aminotransferase specifically requiring α-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 δ-carboxymethyl-α-hydroxymuconic acid which, when supplemented with 2 mol of diphosphopyridine dinucleotide, results in the production of stoichiometric amounts of succinate and pyruvate.
Publisher
Canadian Science Publishing
Subject
Genetics,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Immunology,Microbiology
Cited by
27 articles.
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