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• W1567290634 abstract "A reductive synthesis of phenylpyruvate from phenylacetyl coenzyme A and bicarbonate was obtained in cell-free extracts from the photosynthetic bacterium Chromatium. This phenylpyruvate synthase activity—which appears to be distinct from pyruvate synthase—depends on the reducing power of ferredoxin and requires thiamine pyrophosphate as a coenzyme. Of several ferredoxins assayed, the native ferredoxin from Chromatium was found to be the most effective for phenylpyruvate synthesis. The enzyme extract also catalyzed the conversion of phenylpyruvate to phenylalanine (in the presence of an amino group donor) and the activation of phenylacetate to the phenylacetyl-CoA derivative. Thus, a net synthesis of phenylalanine from phenylacetate and CO2 was accomplished. Closely associated with the phenylpyruvate synthase reaction was an exchange reaction between 14C-bicarbonate and phenylpyruvate. The exchange reaction required thiamine pyrophosphate and CoA as cofactors. Apart from Chromatium, phenylpyruvate synthase and phenylpyruvate-bicarbonate exchange activities were also found in cell-free extracts from the green photosynthetic bacteria Chlorobium thiosulfatophilum and Chloropseudomonas ethylicum." @default.
• W1567290634 created "2016-06-24" @default.
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• W1567290634 date "1971-07-01" @default.
• W1567290634 modified "2023-09-30" @default.
• W1567290634 title "Ferredoxin-dependent Phenylpyruvate Synthesis by Cell-free Preparations of Photosynthetic Bacteria" @default.
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• W1567290634 doi "https://doi.org/10.1016/s0021-9258(18)62042-3" @default.
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