Distinct characteristics of the substrate binding between highly homologous catalase-related allene oxide synthase and hydroperoxide lyase

2019 ◽  
Vol 676 ◽  
pp. 108126
Author(s):  
Tarvi Teder ◽  
Nigulas Samel ◽  
Helike Lõhelaid
Plant Science ◽  
2005 ◽  
Vol 169 (1) ◽  
pp. 139-146 ◽  
Author(s):  
Meshack Afitlhile ◽  
Hirotada Fukushige ◽  
Charles McCraken ◽  
David Hildebrand

2019 ◽  
Vol 20 (12) ◽  
pp. 3064 ◽  
Author(s):  
Sachin Rustgi ◽  
Armin Springer ◽  
ChulHee Kang ◽  
Diter von Wettstein ◽  
Christiane Reinbothe ◽  
...  

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.


2000 ◽  
Vol 28 (6) ◽  
pp. 847-849 ◽  
Author(s):  
D. F. Hildebrand ◽  
M. Afitlhile ◽  
H. Fukushige

Two very common groups of oxylipins formed in plants involve the conversion of fatty acid hydroperoxides, such as hydroperoxy-octadecatrienoic acid, into further metabolites by allene oxide synthase and hydroperoxide lyase. Both of these oxylipin branch pathways appear to be ubiquitous or nearly so in plants, but the relative activities of these two branches vary among plant species. In most plants examined, including Arabidopsis product formation from either of these pathways is minimal until elicited by wounding or some other means, upon which products from both pathways, such as jasmonic acid and C6 aldehydes and alcohols, can increase by orders of magnitude. In some plant species such as Artemisia and Jasminum spp. oxylipin product formation is heavily skewed towards allene oxide synthase products. Others such as watermelon (Citrullus lanatus) produce 10-fold higher amounts or more of hydroperoxide lyase than allene oxide synthase products. Arabidopsis and tobacco are intermediate between these extremes. Artemisia and Jasminum are also unusual in that they do not require wounding or other types of induction for high oxylipin product formation. Release of non-esterified fatty acids appears to be correlated with oxylipin formation, but phospholipase A2 appears not to be involved with oxylipin production, at least in the case of Artemisia leaves.


2022 ◽  
Vol 195 ◽  
pp. 113051
Author(s):  
Yana Y. Toporkova ◽  
Elena K. Askarova ◽  
Svetlana S. Gorina ◽  
Lucia S. Mukhtarova ◽  
Alexander N. Grechkin

FEBS Letters ◽  
2008 ◽  
Vol 582 (23-24) ◽  
pp. 3423-3428 ◽  
Author(s):  
Yana Y. Toporkova ◽  
Yuri V. Gogolev ◽  
Lucia S. Mukhtarova ◽  
Alexander N. Grechkin

2006 ◽  
Vol 281 (51) ◽  
pp. 38981-38988 ◽  
Author(s):  
Bénédicte Bakan ◽  
Mats Hamberg ◽  
Ludivine Perrocheau ◽  
Daniel Maume ◽  
Hélène Rogniaux ◽  
...  

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