Probing the specificity of CYP112 in bacterial gibberellin biosynthesis.

ABSTRACT: Biosynthesis of the gibberellin A (GA) plant hormones evolved independently in plant-associated fungi and bacteria. While the relevant enzymes have distinct evolutionary origins, the pathways proceed via highly similar reactions. One particularly complex transformation involves combined demethylation and γ-lactone ring formation, catalyzed in bacteria by the cytochrome P450 CYP112 in three individual steps, which involves large structural changes in the transition from substrate to product, with further divergence in the recently demonstrated use of two separate mechanistic routes. Here, the substrate specificity of the isozyme from Erwinia tracheiphila, EtCYP112, was probed via UV-Vis spectral binding studies and activity assays with alternate substrates from the GA biosynth

SUBMITTER: Nagel R 

PROVIDER: S-EPMC6035067 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature