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Review

ALLENE OXIDE SYNTHASE and HYDROPEROXIDE LYASE, Two Non-Canonical Cytochrome P450s in Arabidopsis thaliana and Their Different Roles in Plant Defense

1
Department of Plant and Environmental Sciences, Pee Dee Research and Education Center, Clemson University, Florence, SC 29506, USA
2
Department of Crop and Soil Sciences, Washington State University, Pullman, WA 99164, USA
3
Medizinische Biologie und Elektronenmikroskopisches Zentrum (EMZ), Universitätsmedizin Rostock, 18055 Rostock, Germany
4
Department of Chemistry, Biomolecular Crystallography Center, Washington State University, Pullman, WA 99164, USA
5
Biologie Environnementale et Systémique (BEEeSy), Université Grenoble Alpes, BP 53, CEDEX, F-38041 Grenoble, France
6
Centro de Biotecnología y Genómica de Plantas, Universidad Politécnica de Madrid (UPM)—Instituto Nacional de Investigación y Tecnología Agraria y Alimentación (INIA), Campus de Montegancedo, 28223 Pozuelo de Alarcón, Madrid, Spain
*
Authors to whom correspondence should be addressed.
Deceased 13 April 2017.
Int. J. Mol. Sci. 2019, 20(12), 3064; https://doi.org/10.3390/ijms20123064
Received: 29 May 2019 / Revised: 19 June 2019 / Accepted: 20 June 2019 / Published: 23 June 2019
(This article belongs to the Collection Feature Papers in Molecular Plant Sciences)
The channeling of metabolites is an essential step of metabolic regulation in all living organisms. Multifunctional enzymes with defined domains for metabolite compartmentalization are rare, but in many cases, larger assemblies forming multimeric protein complexes operate in defined metabolic shunts. In Arabidopsis thaliana, a multimeric complex was discovered that contains a 13-lipoxygenase and allene oxide synthase (AOS) as well as allene oxide cyclase. All three plant enzymes are localized in chloroplasts, contributing to the biosynthesis of jasmonic acid (JA). JA and its derivatives act as ubiquitous plant defense regulators in responses to both biotic and abiotic stresses. AOS belongs to the superfamily of cytochrome P450 enzymes and is named CYP74A. Another CYP450 in chloroplasts, hydroperoxide lyase (HPL, CYP74B), competes with AOS for the common substrate. The products of the HPL reaction are green leaf volatiles that are involved in the deterrence of insect pests. Both enzymes represent non-canonical CYP450 family members, as they do not depend on O2 and NADPH-dependent CYP450 reductase activities. AOS and HPL activities are crucial for plants to respond to different biotic foes. In this mini-review, we aim to summarize how plants make use of the LOX2–AOS–AOC2 complex in chloroplasts to boost JA biosynthesis over volatile production and how this situation may change in plant communities during mass ingestion by insect pests. View Full-Text
Keywords: allene oxide synthase; allene oxide cyclase; chloroplast envelope protein complex; hydroperoxide lyase; lipoxygenase; metabolite channeling; plant defense allene oxide synthase; allene oxide cyclase; chloroplast envelope protein complex; hydroperoxide lyase; lipoxygenase; metabolite channeling; plant defense
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MDPI and ACS Style

Rustgi, S.; Springer, A.; Kang, C.; von Wettstein, D.; Reinbothe, C.; Reinbothe, S.; Pollmann, S. ALLENE OXIDE SYNTHASE and HYDROPEROXIDE LYASE, Two Non-Canonical Cytochrome P450s in Arabidopsis thaliana and Their Different Roles in Plant Defense. Int. J. Mol. Sci. 2019, 20, 3064. https://doi.org/10.3390/ijms20123064

AMA Style

Rustgi S, Springer A, Kang C, von Wettstein D, Reinbothe C, Reinbothe S, Pollmann S. ALLENE OXIDE SYNTHASE and HYDROPEROXIDE LYASE, Two Non-Canonical Cytochrome P450s in Arabidopsis thaliana and Their Different Roles in Plant Defense. International Journal of Molecular Sciences. 2019; 20(12):3064. https://doi.org/10.3390/ijms20123064

Chicago/Turabian Style

Rustgi, Sachin, Armin Springer, ChulHee Kang, Diter von Wettstein, Christiane Reinbothe, Steffen Reinbothe, and Stephan Pollmann. 2019. "ALLENE OXIDE SYNTHASE and HYDROPEROXIDE LYASE, Two Non-Canonical Cytochrome P450s in Arabidopsis thaliana and Their Different Roles in Plant Defense" International Journal of Molecular Sciences 20, no. 12: 3064. https://doi.org/10.3390/ijms20123064

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