DL-4-hydroxyphenylglycine catabolism in Pseudomonas putida MW27 |
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Authors: | W J J van den Tweel M N Widjojoatmodjo J A M de Bont |
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Institution: | (1) Division of Industrial Microbiology, Department of Food Science, Agricultural University, P. O. Box 8129, NL-6700 EV, Wageningen, The Netherlands;(2) Present address: Bio-organic Chemistry Section, DSM Research, P. O. Box 18, NL-6160 MD Geleen, The Netherlands |
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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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Keywords: | DL-4-Hydroxyphenylglycine" target="_blank">DL-4-Hydroxyphenylglycine Pseudomonas putida Transamination |
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