Unusual intramolecular N-->O acyl group migration occurring during conjugation of (-)-DHMEQ with cysteine.
Previously we found that (-)-DHMEQ, a specific NF-kappaB inhibitor, covalently bound to a specific cysteine of NF-kappaB component proteins. In the course of formation of the (-)-DHMEQ and protected cysteine conjugate, we observed an unusual intramolecular N-->O acyl group migration.
Kozawa
Ikuko
I
Department of Applied Chemistry, Faculty of Science and Technology, Keio University, 3-14-1 Hiyoshi, Kohoku-ku, Yokohama 223-8522, Japan.
Kato
Kuniki
K
Teruya
Toshiaki
T
Suenaga
Kiyotake
K
Umezawa
Kazuo
K
D001549:Benzamides / Q000378:metabolism*; D003512:Cyclohexanones / Q000378:metabolism*; D003545:Cysteine / Q000378:metabolism*; D008968:Molecular Conformation; D016328:NF-kappa B / Q000037:antagonists & inhibitors*
D001549:Benzamides; D003512:Cyclohexanones; D016328:NF-kappa B; C464444:dehydroxymethylepoxyquinomicin; D003545:Cysteine