Abstract
Thirteen bacteria were isolated on D-4-hydroxyphenylglycine as sole carbon and energy source. Seven strains transaminated only the D-enantiomer while the other six isolates transaminated both enantiomers of 4-hydroxyphenylglycine. One of the six strains utilizing both enantiomers was characterized as a Pseudomonas putida. This strain, MW27, employed two enantioselective transaminases, to catalyze the initial step in the metabolism of DL-4-hydroxyphenylglycine. The product of the transamination, 4-hydroxyphenylglyoxylate, was further metabolized via 4-hydroxybenzaldehyde and 4-hydroxybenzoate to protocatechuate. Preliminary results indicate that both transaminases are co-ordinately synthesized together with the 4-hydroxyphenylglyoxylate decarboxylase and the NADP+-dependent 4-hydroxybenzaldehyde dehydrogenase.
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van den Tweel, W.J.J., Widjojoatmodjo, M.N. & de Bont, J.A.M. DL-4-hydroxyphenylglycine catabolism in Pseudomonas putida MW27. Arch. Microbiol. 150, 471–476 (1988). https://doi.org/10.1007/BF00422289
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DOI: https://doi.org/10.1007/BF00422289