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l tyrosine/glycine max
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Effect of NAD(P)H:quinone oxidoreductase on tyrosinase-mediated oxidation of opioid neuropeptides Leu-enkephalin and Met-enkephalin.
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In vitro experiments are reported showing that NAD(P)H:(quinone acceptor) oxidoreductase (QR), purified from Glycine max seedlings, reduces Leu- and Met-enkephalin-tyrosinase oxidation products, in the presence of NADH or NADPH. QR was not capable to catalyze the reduction of N-acetyl-dopaquinone
Reaction Mechanism of Prephenate Dehydrogenase from the Alternative Tyrosine Biosynthesis Pathway in Plants.
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Unlike metazoans, plants, bacteria, and fungi retain the enzymatic machinery necessary to synthesize the three aromatic amino acids l-phenylalanine, l-tyrosine, and l-tryptophan de novo. In legumes, such as soybean, alfalfa, and common bean, prephenate dehydrogenase (PDH) catalyzes the
Non-plastidic, tyrosine-insensitive prephenate dehydrogenases from legumes.
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L-Tyrosine (Tyr) and its plant-derived natural products are essential in both plants and humans. In plants, Tyr is generally assumed to be synthesized in the plastids via arogenate dehydrogenase (TyrA(a), also known also ADH), which is strictly inhibited by L-Tyr. Using phylogenetic and expression
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