12-oxophytodienoate reductase

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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'>
<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/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.
'''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.
*<scene name='71/710043/Cv/16'>12-oxophytodienoate binding site</scene>.
*<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>.
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*<scene name='71/710043/Cv/17'>FMN binding site</scene>. Water molecules are shown as red spheres.
*<scene name='71/710043/Cv/15'>Click here to see whole active site</scene>.
*<scene name='71/710043/Cv/15'>Click here to see whole active site</scene>.
OPR exhibits self inhibition by dimerization.<ref>PMID:11377202</ref> Three isozymes of OPR are known – OPR1, OPR2, OPR3.<br />
OPR exhibits self inhibition by dimerization.<ref>PMID:11377202</ref> Three isozymes of OPR are known – OPR1, OPR2, OPR3.<br />
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== Relevance ==
== Relevance ==
OPR is part of the jasmonic acid synthesis pathway. Jasmonic acid is regulating plant responses to abiotic and biotic stresses.
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>
 
== 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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