Synthesis of a novel inhibitor against MRSA and VRE: preparation from zerumbone ring opening material showing histidine-kinase inhibition.
Zerumbone ring-opening derivative 2 inhibited autophosphorylation of the essential histidine protein kinase (HPK), YycG, existing in Bacillus subtilis constituting a two-component system (TCS). However, it did not inhibit drug-resistant bacterium such as MRSA and VRE. Tryptophan derivative 34 also could be regulated by a TCS system like 2. In addition, 34 showed good inhibition against MRSA and VRE.
Kitayama
Takashi
T
Department of Advanced Bioscience, Graduate School of Agriculture, Kinki University, Nara 631-8505, Japan. kitayama@nara.kindai.ac.jp
Iwabuchi
Risa
R
Minagawa
Shu
S
Sawada
Seiji
S
Okumura
Ryo
R
Hoshino
Kazuki
K
Cappiello
John
J
Utsumi
Ryutaro
R
D001412:Bacillus subtilis / Q000201:enzymology; D013293:Enterococcus faecalis / Q000187:drug effects*; D000071677:Histidine Kinase; D016106:Methicillin Resistance / Q000187:drug effects*; D008826:Microbial Sensitivity Tests; D010766:Phosphorylation; D011494:Protein Kinases / Q000187:drug effects*; D012717:Sesquiterpenes / Q000138:chemical synthesis* / Q000494:pharmacology*; D013211:Staphylococcus aureus / Q000187:drug effects* / Q000201:enzymology; D014364:Tryptophan / Q000031:analogs & derivatives / Q000494:pharmacology
D012717:Sesquiterpenes; C403304:zerumbone; D014364:Tryptophan; D011494:Protein Kinases; D000071677:Histidine Kinase