A new type of tripropeptin with anteiso-branched chain fatty acid from Lysobacter sp. BMK333-48F3.
Branched chain amino acids are often utilized as the precursors of many lipid-containing bacterial secondary metabolites. The effect of isoleucine on the composition of the mixture of cyclic lipopeptide antibiotics, tripropeptins from Lysobacter sp. BMK333-48F3 was evaluated. As expected, a novel tripropeptin analog with an anteiso-branched fatty acid was produced. The new compound, TPPaiC shows potent antibacterial activity against Gram-positive bacteria including MRSA and VRE. On the other hand, no increase was observed in the production of other tripropeptins by the addition of isoleucine.
Hashizume
Hideki
H
Microbial Chemistry Research Center, 3-14-23 Kamiosaki, Shinagawa-ku, Tokyo 141-0021, Japan. hashizumeh@bikaken.or.jp
Igarashi
Masayuki
M
Sawa
Ryuichi
R
Adachi
Hayamitsu
H
Nishimura
Yoshio
Y
Akamatsu
Yuzuru
Y
D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D047630:Depsipeptides / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D005227:Fatty Acids / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D005285:Fermentation; D053528:Lysobacter / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy
D000900:Anti-Bacterial Agents; D047630:Depsipeptides; D005227:Fatty Acids; C535087:tripropeptin aiC