Indoleacetic Acid Oxidase: A Dual Catalytic Enzyme?

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Promotion of indoleacetic Acid oxidase isoenzymes in tobacco callus cultures by indoleacetic Acid.

Indoleacetic acid oxidase in tobacco callus cultures (Nicotiana tabacum L., cv. White Gold) was composed of at least two groups of isoenzymes, which were distinctly different in electrophoretic mobilities and in responses to growth substances. Indoleacetic acid had dual effects; at low concentrations it promoted the development of two fast-migrating indoleacetic acid oxidase isoenzymes, but at ...

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The coenzyme requirement and enzyme inhibitors of pineapple indoleacetic acid oxidase.

E&acts of pineapple stem tissue constitute the most potent known source of indoleacetic acid oxidase, despite the presence of an inhibitor which is difficult to remove without simultaneously removing some other factor necessary for maximal activity (I). Dialysis invariably lowers the enzyme activity as compared with photolysis, and even prolonged photolysis is never completely effective in remo...

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Indoleacetic acid oxidase and an inhibitor in pineapple tissue.

Tang and Bonner (16) have described an indoleacetic acid (IAA) oxidase system in pea epicotyls, and also an IAA oxidase inhibitor (17). These findings have been confirmed and extended by others (5-8, 18) and an IAA oxidase has been found in several plants, including beans (18) and pineapple leaf tissue (9). The presence of an inhibitor of IAA oxidation has not previously been shown in the pinea...

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Isolation and properties of the enzyme system forming indoleacetic Acid.

The enzymatic conversion of tryptophan to ind,oleacetic acid (IAA) has been demonstrated in lower and higher plants. In some plants the pathway muist be limited to that involving ini(olepyrtuvic acid (5 ) while in others an alterniative pathway involving tryptamine also exists (6, Q). Alth,ouigh the enzyme system from the pineapple leaf converting tryptophlan and tryptamine to auixin was obtain...

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ژورنال

عنوان ژورنال: Plant Physiology

سال: 1972

ISSN: 0032-0889,1532-2548

DOI: 10.1104/pp.50.1.15