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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.