K1115 A, a new anthraquinone that inhibits the binding of activator protein-1 (AP-1) to its recognition sites. II. Taxonomy, fermentation, isolation, physico-chemical properties and structure determination.
A new inhibitor of the action of activator protein-1 (AP-1), designated K1115 A, was isolated from the fermentation broth of an actinomycete strain Mer-K1115. K1115 A was determined to be a new anthraquinone, 3,8-dihydroxy-1-propylanthraquinone-2-carboxylic acid, based on spectroscopic analysis, derivatization experiments and biosynthetic studies with 13C-enriched acetic acid. Two co-produced compounds, K1115 B1 and B2, were also isolated and characterized as new members of the naphthopyranomycin and exfoliamycin group.
Tsukuba Research Laboratories, Eisai Co. Ltd., Ibaraki, Japan.
N
N
Naruse
M
M
Goto
Y
Y
Watanabe
T
T
Terasawa
K
K
Dobashi
D000880:Anthraquinones / Q000138:chemical synthesis* / Q000737:chemistry* / Q000302:isolation & purification*; D005285:Fermentation; D009682:Magnetic Resonance Spectroscopy; D011500:Protein Synthesis Inhibitors / Q000737:chemistry* / Q000302:isolation & purification*; D013055:Spectrophotometry, Infrared; D013302:Streptomyces / Q000145:classification / Q000378:metabolism*; D018808:Transcription Factor AP-1 / Q000378:metabolism
D000880:Anthraquinones; C114112:K 1115 A; D011500:Protein Synthesis Inhibitors; D018808:Transcription Factor AP-1