Molecular cloning and functional expression of gibberellin 2- oxidases, multifunctional enzymes involved in gibberellin deactivation.

ABSTRACT: A major catabolic pathway for the gibberellins (GAs) is initiated by 2beta-hydroxylation, a reaction catalyzed by 2-oxoglutarate-dependent dioxygenases. To isolate a GA 2beta-hydroxylase cDNA clone we used functional screening of a cDNA library from developing cotyledons of runner bean (Phaseolus coccineus L.) with a highly sensitive tritium-release assay for enzyme activity. The encoded protein, obtained by heterologous expression in Escherichia coli, converted GA9 to GA51 (2beta-hydroxyGA9) and GA51-catabolite, the latter produced from GA51 by further oxidation at C-2. The enzyme thus is multifunctional and is best described as a GA 2-oxidase. The recombinant enzyme also 2beta-hydroxylated other C19-GAs, although only GA9 and GA4 were converted to the corresponding catabolites. Three rel

SUBMITTER: Thomas SG 

PROVIDER: S-EPMC16395 | biostudies-literature | 1999 Apr

REPOSITORIES: biostudies-literature