Characterization of novel imidazole derivative, JM‐8686, a potent inhibitor of allene oxide synthase | Zendy

Oh Keimei | Zendy; Asami Tadao | Zendy; Matsui Kenji | Zendy; Howe Gregg A. | Zendy; Murofushi Noboru | Zendy

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Characterization of novel imidazole derivative, JM‐8686, a potent inhibitor of allene oxide synthase

Author(s) -

Oh Keimei,

Asami Tadao,

Matsui Kenji,

Howe Gregg A.,

Murofushi Noboru

Publication year - 2006

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2006.09.044

Subject(s) - allene , chemistry , stereochemistry , nitric oxide synthase , atp synthase , biosynthesis , derivative (finance) , enzyme , biochemistry , catalysis , financial economics , economics

The inhibitory properties of a first synthetic jasmonic acid biosynthesis inhibitor, JM‐8686, were investigated. Steady‐state kinetic analysis indicates that the compound is a competitive inhibitor of allene oxide synthase (AOS) with a K i value of approximate 0.62 ± 0.15 μM. Dialysis experiment indicates that AOS inactivation by JM‐8686 is reversible. The optical difference spectroscopy analysis of JM‐8686 and AOS interaction indicates that JM‐8686 induced type II binding spectra with a K d value of approximate 1.6 ± 0.2 μM, suggesting that JM‐8686 binds to the prosthetic heme iron of AOS. Comparison of the inhibitory potency of the compound against HPL (CYP74B) from tomato revealed that JM‐8686 was a highly selective inhibitor for AOS.

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