Crystal structure of Arabidopsis thaliana 12-oxophytodienoate reductase isoform 3 in complex with 8-iso prostaglandin A(1).

12-Oxophytodienoate reductase 3 (OPR3), one of the enzymes involved in the biosynthesis of the plant hormone jasmonic acid (JA), catalyzes the reduction of the cyclopentenone ring of (9,13)-12-oxophytodienoate [(9,13)-OPDA]. However, there has been no structural information about the interaction between OPRs and the physiologically relevant (9,13)-OPDA. Here we report the crystal structure of OPR3 in complex with 8- prostaglandin A1 (8- PGA) which has the same stereochemistry in the cyclopentenone ring as in the physiologically relevant 9,13-OPDA.

Transformation of RDX and other energetic compounds by xenobiotic reductases XenA and XenB.

The transformation of explosives, including hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX), by xenobiotic reductases XenA and XenB (and the bacterial strains harboring these enzymes) under both aerobic and anaerobic conditions was assessed. Under anaerobic conditions, Pseudomonas fluorescens I-C (XenB) degraded RDX faster than Pseudomonas putida II-B (XenA), and transformation occurred when the cells were supplied with sources of both carbon (succinate) and nitrogen (NH4+), but not when only carbon was supplied. Transformation was always faster under anaerobic conditions compared to aerobic conditions, with both enzymes exhibiting a O2 concentration-dependent inhibition of RDX transformation.