AI Article Synopsis
- A new synthetic compound, JM-8686, has been found to inhibit the enzyme allene oxide synthase (AOS), which is important for jasmonic acid biosynthesis.
- The compound acts as a competitive inhibitor with a measured inhibition constant (K(i)) of about 0.62 µM, and its binding effect on AOS is reversible.
- JM-8686 shows selective inhibition for AOS over another enzyme, HPL, with a binding affinity (K(d)) of approximately 1.6 µM, indicating it binds specifically to the heme iron in AOS.
Article Abstract
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 microM. 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 microM, 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.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.febslet.2006.09.044 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!