ArticleBMB reports2013
Dual positional substrate specificity of rice allene oxide synthase-1: insight into mechanism of inhibition by type II ligand imidazole.
Article in BMB reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Plant oxylipins: adaptation to environmental stresses and impact on mycotoxin contamination.Frontiers in plant science · 2025Review
- Role of Cytochrome P450 Enzyme in Plant Microorganisms' Communication: A Focus on Grapevine.International journal of molecular sciences · 2023Review
- Zucchini Plants Alter Gene Expression and Emission of (Frontiers in plant science · 2020Article
- Jasmonates: News on Occurrence, Biosynthesis, Metabolism and Action of an Ancient Group of Signaling Compounds.International journal of molecular sciences · 2018Review
- Structural Evidence for the Substrate Channeling of Rice Allene Oxide Cyclase in Biologically Analogous Nazarov Reaction.Frontiers in chemistry · 2018Article
- Synthesis and Functions of Jasmonates in Maize.Plants (Basel, Switzerland) · 2016Review
- Cellular localization and detergent dependent oligomerization of rice allene oxide synthase-1.Journal of plant research · 2015Article
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Authors and funding
3 authors.
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Abstract
Phylogenetic and amino acid sequence analysis indicated that rice allene oxide synthase-1 (OsAOS1) is CYP74, and is clearly distinct from CYP74B, C and D subfamilies. Regio- and stereo-chemical analysis revealed the dual substrate specificity of OsAOS1 for (cis,trans)-configurational isomers of 13(S)- and 9(S)-hydroperoxyoctadecadienoic acid. GC-MS analysis showed that OsAOS1 converts 13(S)- and 9(S)-hydroperoxyoctadecadi(tri)enoic acid into their corresponding allene oxide. UV-Visible spectral analysis of native OsAOS1 revealed a Soret maximum at 393 nm, which shifted to 424 nm with several clean isobestic points upon binding of OsAOS1 to imidazole. The spectral shift induced by imidazole correlated with inhibition of OsAOS1 activity, implying that imidazole may coordinate to ferric heme iron, triggering a heme-iron transition from high spin state to low spin state. The implications and significance of a putative type II ligand-induced spin state transition in OsAOS1 are discussed.
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