Abstract
Abstract The reduction of 3-methyleneoxindole, a biologically active metabolite of natural plant auxin, to the inert 3-methyloxindole is catalyzed by four or five reduced triphosphopyridine nucleotide-linked enzymes. Two of the reductases, which can be separated completely by column chromatography, exhibit differential sensitivity to the synthetic auxins, 1-naphthaleneacetic acid and 2,4-dichlorophenoxyacetic acid. Reductase A is inhibited noncompetitively by 2,4-dichlorophenoxyacetic acid which is a weak competitive inhibitor of reductase B. Reductase B, on the other hand, is inhibited competitively by 1-naphthaleneacetic acid, a weak competitive inhibitor of reductase A. Reductase A is labile, losing activity as well as its pH-dependent sensitivity to 2,4-dichlorophenoxyacetic acid. Reductase B is stable, and its inhibition by the synthetic auxins is pH independent.
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