Involvement of 4-hydroxymandelic acid in the degradation of mandelic acid by Pseudomonas convexa.
A microorganism capable of degrading DL-mandelic acid was isolated from sewage sediment of enrichment culture and was identified as Pseudomonas convexa. It was found to metabolize mandelic acid by a new pathway involving 4-hydroxymandelic acid, 4-hydroxybenzaldehyde, 4-hydroxybenzoic acid, and 3,4-dihydroxybenzoic acid as aromatic intermediates. All the enzymes of the pathway were demonstrated in cell-free extracts. L-Mandelate-4-hydroxylase, a soluble enzyme, requires tetrahydropteridine, nicotinamide adenine dinucleotide phosphate, reduced form, and Fe2+ for its activity. The next enzyme, L-4-hydroxymandelate oxidase (decarboxylating), a particulate enzyme, requires flavine adenine dinucleotide and Mn2+ for its activity. A nicotinamide adenine dinucleotide-dependent, as well as a nicotinamide adenine dinucleotide phosphate-dependent, benzaldehyde dehydrogenase has been resolved and partially purified.
D002262:Carboxy-Lyases / Q000378:metabolism; D002474:Cell-Free System; D004790:Enzyme Induction; D005947:Glucose / Q000494:pharmacology; D008333:Mandelic Acids / Q000378:metabolism*; D006899:Mixed Function Oxygenases / Q000378:metabolism; D010088:Oxidoreductases / Q000378:metabolism; D010101:Oxygen Consumption; D011549:Pseudomonas / Q000201:enzymology / Q000378:metabolism*; D019998:Racemases and Epimerases / Q000378:metabolism
D008333:Mandelic Acids; D006899:Mixed Function Oxygenases; D010088:Oxidoreductases; D002262:Carboxy-Lyases; D019998:Racemases and Epimerases; D005947:Glucose