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- W2127223896 abstract "The transaminations of L-tryptophan (L-trp) and of L-phenylalanine (L-phe) are catalysedin vitro by the same non-specific aminotransferase. The transaminations procceed at the same pH (pH 8.5) and temperature (45 °C) optima, have parallel increases in activity with addition of the coenzyme pyridoxal phosphate (PRP) and have identical elution characteristics in gel chromatography. The enzyme from pea seedlings has a relatively weak affinity for both amino acids (Km L-trp = 4.16 à 10-1 mmol 1-1; Km L-phe = 2.10 à 10-1 mmol 1-1). Differences in affinity for a series of keto acids in the pea enzyme were observed, with pyruvate having the strongest and glyoxylate the weakest affinity. Transamination of L-trp and L-phe was demonstrated by enzyme extracts from pea, maize and tomato, but was not detected in kohlrabi. The amino acids L-asparagine (L-asn), L-phe, L-lysine (L-lys), L-methionine (L-met) have distinct inhibitory effects on the transamination of L-trp. Indolylacetylaspartate and tryptophol were shown to be competitive inhibitors. The regulation at the molecular level of L-trp transaminase activity is discussed." @default.
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- W2127223896 date "1991-07-01" @default.
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- W2127223896 title "Enzymes of auxin biosynthesis and their regulation I. Tryptophan and phenylalanine aminotransferase in pea plants" @default.
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- W2127223896 doi "https://doi.org/10.1007/bf02885374" @default.
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