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Metabolism and Enzymology

Partial Purification and Characterization of the Gibberellin A₂₀ 3-Hydroxylase from Seeds of Phaseolus vulgaris¹

School of Chemistry, University of Bristol, Bristol BS8 1TS, United Kingdom

The GA₂₀ 3-hydroxylase present in immature seeds of Phaseolus vulgaris has been partially purified and characterized. The physical characteristics of the enzyme are similar to those of the GA 2-hydroxylases present in mature and immature seeds of Pisum sativum. It is acid-labile, hydrophobic, and of M_r 45,000. The enzyme catalyzes the synthesis of GA₁, GA₅, and GA₂₉ from GA₂₀. Activity is dependent upon the presence of Fe²⁺, ascorbate, 2-oxoglutarate, and oxygen. 2-Oxoglutarate does not function as a cosubstrate; in the presence of the enzyme, succinate is not a reaction product.

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