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- W2014869923 abstract "Abstract This paper deals with some properties of enzymes involved in the synthesis of phenolic acids, with special reference to their intracellular location. The results obtained can be summarized as follows: 1. 1. Two phenylalanine ammonia-lyase isoenzymes coexist in Quercus roots as has been previously described for oak leaves. The cinnamate-sensitive isoenzyme is associated with the microsomal fraction whereas the benzoate-sensitive isoenzyme is located in the “F 10 000” fraction including mitochondria and microbodies. 2. 2. The cinnamate 4-hydroxylase, catalyzing p-coumarate formation, is tightly bound to microsomes and the “benzoate synthase”, an emzyme involved in the benzoic acid formation from t-cinnamate, is confined to the “F 10 000” fraction, presumably in microbodies. These data show that phenolic acids biosynthesis pathways are closely compartmented in organelles so that phenylpropanoid compounds are mainly formed in microsomes whereas C6−C1 acids are formed in microbodies. The regulation of these pathways seems to involve sophisticated mechanisms, associating isoenzymes with tight compartments." @default.
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- W2014869923 date "1972-09-15" @default.
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- W2014869923 title "Recherches sur les enzymes catalysant la formation des acides phénoliques chez Quercus pedunculata (EHRH.) II. Localisation intracellulaire de la phenylalanine ammoniaque-lyase, de la cinnamate 4-hydroxylase, et de la “benzoate synthase”" @default.
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- W2014869923 doi "https://doi.org/10.1016/0304-4165(72)90144-4" @default.
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