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   <subfield code="a">The involvement of an enantioselective transaminase in the metabolism of D-3- and D-4-hydroxyphenylglycine in Pseudomonas putida LW-4</subfield>
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   <subfield code="a">Summary: Pseudomonas putida LW-4, isolated on D-phenylglycine as sole carbon and energy source, was also able to grow on D-3-and D-4-hydroxyphenylglycine. Both D-3-and D-4-hydroxyphenylglycine were initially converted to the corresponding hydroxyphenylglyoxylates by means of an enantioselective transaminase. Subsequently, the hydroxyphenylglyoxylates were decarboxylated and then oxidized to 3-and 4-hydroxybenzoate, respectively. These latter compounds in turn were oxidized by NADPH-dependent hydroxylases to protocatechuate, which was further oxidized via an intradiol cleavage. Preliminary experiments with cell extracts in which the 4-hydroxyphenylglyoxylate decarboxylase was partially removed by an ammonium sulfate fractionation showed that D-4-hydroxyphenylglyoxycine could be formed from 4-hydroxyphenylglyoxylate by the enantioselective transaminase.</subfield>
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