Unknown

Dataset Information

0

Labeling Studies Clarify the Committed Step in Bacterial Gibberellin Biosynthesis.


ABSTRACT: Bacteria have evolved gibberellin phytohormone biosynthesis independently of plants and fungi. Through 13C-labeling and NMR analysis, the mechanistically unusual "B" ring contraction catalyzed by a cytochrome P450 (CYP114), which is the committed step in gibberellin biosynthesis, was shown to occur via oxidative extrusion of carbon-7 from ent-kaurenoic acid in bacteria. This is identical to the convergently evolved chemical transformation in plants and fungi, suggesting a common semipinacol rearrangement mechanism potentially guided by carbon-4α carboxylate proximity.

SUBMITTER: Nett RS 

PROVIDER: S-EPMC5139915 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Labeling Studies Clarify the Committed Step in Bacterial Gibberellin Biosynthesis.

Nett Ryan S RS   Dickschat Jeroen S JS   Peters Reuben J RJ  

Organic letters 20161121 23


Bacteria have evolved gibberellin phytohormone biosynthesis independently of plants and fungi. Through <sup>13</sup>C-labeling and NMR analysis, the mechanistically unusual "B" ring contraction catalyzed by a cytochrome P450 (CYP114), which is the committed step in gibberellin biosynthesis, was shown to occur via oxidative extrusion of carbon-7 from ent-kaurenoic acid in bacteria. This is identical to the convergently evolved chemical transformation in plants and fungi, suggesting a common semip  ...[more]

Similar Datasets

| S-EPMC5700162 | biostudies-literature
| S-EPMC11602165 | biostudies-literature
| S-EPMC6035067 | biostudies-literature
| S-EPMC5165104 | biostudies-literature
| S-EPMC2914249 | biostudies-literature
| S-EPMC3283191 | biostudies-literature
| S-EPMC6391936 | biostudies-literature
| S-EPMC6020689 | biostudies-literature
| S-EPMC10293830 | biostudies-literature
| S-EPMC8538045 | biostudies-literature