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Flavobacterium F24 metabolized both stereoisomers of phenylglycine and enzyme studies revealed that l-phenylglycine was transaminated by a constitutive enzyme while the d-stereoisomer was oxidized by a phenazine-methosulphate-dependent d-amino-acid dehydrogenase. This latter enzyme was not induced during growth on l-phenylglycine. Phenylglyoxylate formed in the reactions was decarboxylated by an inducible enzyme to benzaldehyde, which was oxidized mainly by an inducible phenazine-methosulphate-dependent benzaldehyde dehydrogenase not described earlier. Benzoate was further metabolized via 3-hydroxybenzoate to gentisate, which in turn was further degraded through a glutathione-dependent pathway.
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