Trierixin, a novel Inhibitor of ER stress-induced XBP1 activation from Streptomyces sp. II. structure elucidation.
Trierixin, a new member of the triene-ansamycin group, has been isolated from the fermentation broth of Streptomyces sp. AC654 as an inhibitor of ER stress-induced XBP1 activation. The structure of trierixin was determined on the basis of its spectroscopical and chemical properties. Trierixin possessed a 21-membered macrocyclic lactam, which contains a methylthio-benzenediol structure, and a cyclohexanecarbonylalanine moiety. Trierixin is thus elucidated as 21-thiomethylmycotrienin II.
Futamura
Yushi
Y
Department of Bioscience and Informatics, Faculty of Science and Technology, Keio University, Yokohama, Japan.
Tashiro
Etsu
E
Hironiwa
Naoka
N
Kohno
Jun
J
Nishio
Maki
M
Shindo
Kazutoshi
K
Imoto
Masaya
M
D004268:DNA-Binding Proteins / Q000037:antagonists & inhibitors; D005285:Fermentation; D006367:HeLa Cells; D006801:Humans; D006873:Hydroquinones / Q000737:chemistry / Q000302:isolation & purification; D047029:Lactams, Macrocyclic / Q000737:chemistry* / Q000302:isolation & purification; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D009687:Nuclear Proteins / Q000037:antagonists & inhibitors; D009904:Optical Rotation; D000071701:Regulatory Factor X Transcription Factors; D013056:Spectrophotometry, Ultraviolet; D013302:Streptomyces / Q000737:chemistry*; D014157:Transcription Factors; D044366:Transition Temperature; D000071717:X-Box Binding Protein 1
D004268:DNA-Binding Proteins; D006873:Hydroquinones; D047029:Lactams, Macrocyclic; D009687:Nuclear Proteins; D000071701:Regulatory Factor X Transcription Factors; D014157:Transcription Factors; D000071717:X-Box Binding Protein 1; C000605543:XBP1 protein, human; C525271:trierixin; C036971:mycotrienin II