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Gene Review:

OPR1 - 12-oxophytodienoate reductase

Solanum lycopersicum

Strassner, J. et al., Breithaupt, C. et al.

Breithaupt, Strassner, Breitinger, Huber, Macheroux, Schaller, Clausen,

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High impact information on opr

The catalytic efficiency of LeOPR was highest with N-ethylmaleimide followed by 12-oxophytodienoic acid and maleic acid as substrates [1].
The ligand binding properties were compared between LeOPR and OYE, and the findings are discussed with respect to structural differences between the active sites of OYE and LeOPR [1].
Photoreduction of the LeOPR-bound FMN resulted in the formation of a red, anionic semiquinone prior to the formation of the fully reduced flavin dihydroquinone [1].
The specific binding of 9R,13R-OPDA by OPR1 explains the experimentally observed stereoselectivity and argues in favor of 9R,13R-OPDA or a structurally related oxylipin as natural substrate of OPR1 [2].
RESULTS: Here, we report the high-resolution crystal structure of OPR1 from Lycopersicon esculentum and its complex structures with the substrate 9R,13R-OPDA and with polyethylene glycol 400 [2].

Analytical, diagnostic and therapeutic context of opr

Spectroscopic characterization of LeOPR revealed the formation of charge transfer complexes upon titration with para-substituted phenolic compounds, a distinctive feature of the enzymes of the OYE family [1].

References

A homolog of old yellow enzyme in tomato. Spectral properties and substrate specificity of the recombinant protein. Strassner, J., Fürholz, A., Macheroux, P., Amrhein, N., Schaller, A. J. Biol. Chem. (1999) [Pubmed]
X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE. Breithaupt, C., Strassner, J., Breitinger, U., Huber, R., Macheroux, P., Schaller, A., Clausen, T. Structure (Camb.) (2001) [Pubmed]

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