Unprecedented olefin-dependent histidine-kinase inhibitory of zerumbone ring-opening material.
Zerumbone ring-opening derivative, 4 (10E/10Z=3/2), inhibited autophosphorylation of the essential histidine-kinase YycG existing in Bacillus subtilis constituting a two-component system (TCS). Generation of 4E-form could be regulated chemically using the difference from the ring-opening reactivity of the precursor forming of 4 and pure 4E was isolated. The stereoisomer, 4E, showed main inhibition activity of autophosphorylation of YycG (IC(50)=63.5 microM).
Kitayama
Takashi
T
Advanced Life Science, Graduate School of Agriculture, Kinki University, Nara 631-8505, Japan.
Iwabuchi
Risa
R
Minagawa
Shu
S
Shiomi
Fumihiro
F
Cappiello
John
J
Sawada
Seiji
S
Utsumi
Ryutaro
R
Okamoto
Tadashi
T
D000475:Alkenes / Q000737:chemistry* / Q000302:isolation & purification; D000071677:Histidine Kinase; D047428:Protein Kinase Inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D011494:Protein Kinases / Q000378:metabolism*; D012717:Sesquiterpenes / Q000737:chemistry* / Q000302:isolation & purification; D013237:Stereoisomerism
D000475:Alkenes; D047428:Protein Kinase Inhibitors; D012717:Sesquiterpenes; C403304:zerumbone; D011494:Protein Kinases; D000071677:Histidine Kinase