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. 1990 Nov;94(3):1390–1401. doi: 10.1104/pp.94.3.1390

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

Valerie A Smith 1, Paul Gaskin 1, Jake MacMillan 1
PMCID: PMC1077389  PMID: 16667844

Abstract

The GA20 3β-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 2β-hydroxylases present in mature and immature seeds of Pisum sativum. It is acid-labile, hydrophobic, and of Mr 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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Selected References

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