In vitro oxidative decarboxylation of L-2-hydroxy-4-methylthiobutanoic acid by L-2-hydroxy acid oxidase A from chicken liver
Autor: | Anne Ferjancic-Biagini, J. De Caro, Liliane Dupuis, Antoine Puigserver |
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Rok vydání: | 1995 |
Předmět: |
Magnetic Resonance Spectroscopy
Decarboxylation Stereochemistry Flavin mononucleotide Flavin group Biochemistry Mass Spectrometry Cofactor chemistry.chemical_compound Methionine Spectroscopy Fourier Transform Infrared Animals Methionine synthase Chromatography High Pressure Liquid Oxidative decarboxylation Oxidase test biology General Medicine Alcohol Oxidoreductases Kinetics Liver chemistry biology.protein Propionates Chickens Oxidation-Reduction |
Zdroj: | Biochimie. 77:249-255 |
ISSN: | 0300-9084 |
DOI: | 10.1016/0300-9084(96)88132-6 |
Popis: | The first step in the set of reactions responsible for the biological utilization of L-2-hydroxy-4-methylthiobutanoic acid, the methionine hydroxy analogue, in protein synthesis was investigated in vitro using pure L-2-hydroxy acid oxidase A from chicken liver. The reaction yielded no more than 20% of the corresponding α-keto acid, 2-keto-4-methylthiobutanoic acid, the well-known intermediate in methionine metabolism, and as much as 80% of the subsequent decarboxylation product, 3-methylthiopropionate, suggesting that L-2-hydroxy-4-methylthiobutanoic acid cannot be completely converted into methionine in vivo . It was therefore concluded that chicken liver L-2-hydroxy acid oxidase, a peroxisomal enzyme requiring flavin mononucleotide as a coenzyme, also has an oxidative decarboxylation activity in vitro , which was found to be NADH-dependent. The mechanism possibly underlying the successive conversion of the methionine hydroxy analogue into α-keto acid and 3-methylthiopropionate by this NADH:flavin oxido-reductase-decarboxylase activity is described. |
Databáze: | OpenAIRE |
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