Aromatic biosynthesis in higher plants. 1. Preparation and properties of dehydroshikimic reductase

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Abstract
A triphosphopyridine nucleotide-linked enzyme catalysing the interconversion of dehydroshikimic acid and shikimic acid was extracted and purified from etiolated epicotyls of pea seedlings. An overall purification of 78-fold was obtained. The pH optimum for the oxidation of shikimic acid was found to be 10''0. The Michaelis constant for shikimic acid at pH 9''0 was 0.19-0.28mM. The Michaelis constant for triphosphopyridine nucleotide at pH 9.0 was 7[mu]M. The purified enzyme preparation appeared to have no multivalent-ion requirement. The enzyme was inhibited by p-chloromercuribenzoate with reversal of inhibition by cysteine. Iodoacetate was slightly inhibitory.