12-oxophytodienoate reductase

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<StructureSection load='1icq' size='340' side='right' caption='Tomato OPR1 complex with FMN (cyan) and 12-oxophytodienoate (green), (PDB code [[1icq]])' scene='71/710043/Cv/6'>
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<StructureSection load='' size='400' side='right' caption='Tomato OPR1 complex with FMN (cyan) and 12-oxophytodienoate (green), (PDB code [[1icq]])' scene='71/710043/Cv/18'>
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__TOC__
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== Introduction ==
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'''12-Oxophytodienoate reductase''' (OPR) is an enzyme that plays a key role in the biosynthesis of jasmonic acid (JA), a plant hormone involved in various physiological processes, including defense responses, growth regulation, and development. OPR catalyzes the reduction of 12-oxo-phytodienoic acid (OPDA) to produce the biologically active JA.
== Function ==
== Function ==
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'''12-oxophytodienoate reductase''' (OPR) catalyzes the conversion of <scene name='71/710043/Cv/7'>12-oxophytodienoate</scene> <span style="color:lime;background-color:black;font-weight:bold;">(green)</span> to 3-oxo-pentenyl-cyclopentane octanoate. The expression of OPR is induced by stimuli like touch, wind, wounding, UV light and detergent. OPR uses the cofactor <scene name='71/710043/Cv/8'>flavin mononucleotide (FMN)</scene> <span style="color:cyan;background-color:black;font-weight:bold;">(cyan)</span> which is reduced by NADPH. <scene name='71/710043/Cv/10'>Click here to see active site</scene>. OPR exhibits self inhibition by dimerization.<ref>PMID:11377202</ref> Three isozymes of OPR are known – OPR1, OPR2, OPR3.<br />
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'''12-oxophytodienoate reductase''' (OPR) catalyzes the conversion of <scene name='71/710043/Cv/11'>12-oxophytodienoate</scene> <span style="color:lime;background-color:black;font-weight:bold;">(green)</span> to 3-oxo-pentenyl-cyclopentane octanoate. The expression of OPR is induced by stimuli like touch, wind, wounding, UV light and detergent. OPR uses the cofactor <scene name='71/710043/Cv/12'>flavin mononucleotide (FMN)</scene> <span style="color:cyan;background-color:black;font-weight:bold;">(cyan)</span> which is reduced by NADPH.
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*<scene name='71/710043/Cv/16'>12-oxophytodienoate binding site</scene>.
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*<scene name='71/710043/Cv/17'>FMN binding site</scene>. Water molecules are shown as red spheres.
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*<scene name='71/710043/Cv/15'>Click here to see whole active site</scene>.
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OPR exhibits self inhibition by dimerization.<ref>PMID:11377202</ref> Three isozymes of OPR are known – OPR1, OPR2, OPR3.<br />
* OPR1 cleaves olefinic bonds in α,β-unsaturated carbonyls.<br />
* OPR1 cleaves olefinic bonds in α,β-unsaturated carbonyls.<br />
* OPR3 cleaves olefinic bonds in cyclic enones.
* OPR3 cleaves olefinic bonds in cyclic enones.
== Relevance ==
== Relevance ==
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OPR is part of the jasmonic acid synthesis pathway. Jasmonic acid is regulating plant responses to abiotic and biotic stresses.
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OPR is part of the jasmonic acid synthesis pathway. Jasmonic acid is regulating plant responses to abiotic and biotic stresses.
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</StructureSection>
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== 3D Structures of 12-oxophytodienoate reductase ==
== 3D Structures of 12-oxophytodienoate reductase ==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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[[12-oxophytodienoate reductase 3D structures]]
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*OPR1
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</StructureSection>
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**[[1icp]], [[1ics]] – tOPR1 (mutant) + FMN – tomato<br />
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**[[1icq]] – tOPR1 (mutant) + FMN + 12-oxophytodienoate<br />
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**[[1vji]], [[2q3r]] – AtOPR1 + FMN – ''Arabidopsis thaliana''<br />
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**[[3hgr]] – tOPR1 (mutant) + FMN + hydroxybenzoate<br />
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*OPR3
 
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**[[1q45]], [[2q3o]] – AtOPR3 + FMN <br />
 
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**[[2hsa]] – tOPR3 + FMN <br />
 
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**[[2hs6]], [[2hs8]], [[3hgo]] – tOPR3 (mutant) + FMN <br />
 
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**[[2g5w]] – AtOPR3 + FMN + 8-iso prostaglandin A1<br />
 
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**[[3hgs]] – tOPR3 + FMN + hydroxybenzoate<br />
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category: Topic Page]]
[[Category: Topic Page]]

Current revision

Tomato OPR1 complex with FMN (cyan) and 12-oxophytodienoate (green), (PDB code 1icq)

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References

  1. Breithaupt C, Strassner J, Breitinger U, Huber R, Macheroux P, Schaller A, Clausen T. X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE. Structure. 2001 May 9;9(5):419-29. PMID:11377202

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Alexander Berchansky, Michal Harel, Joel L. Sussman

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