Acylpeptides, the inhibitors of cyclic adenosine 3',5'-monophosphate phosphodiesterase. I. Purification, physicochemical properties and structures of fatty acid residues.
An inhibitor of cyclic adenosine 3',5'-monophosphate (cAMP) phosphodiesterase was isolated from the culture filtrate of Bacillus subtilis C-756 isolated from soil. It was purified and finally separated into three fractions by reverse-phase HPLC. The respective fractions were designated as APD-I, -II and -III in the order eluted and the relative quantities of APD-I, -II and -III were approximately 10%, 40% and 50%, respectively. They were acylpeptides composed of beta-hydroxy fatty acid residues and heptapeptide. Though the amino acid compositions of the peptides were the same, the fatty acid residues were all different. APD-I contained a mixture of 3-hydroxy-11-methyldodecanoic acid (i-C13h3) and 3-hydroxy-10-methyldodecanoic acid (a-C13h3). APD-II contained 3-hydroxytetradecanoic acid (n-C14h3). APD-III contained a mixture of 3-hydroxy-13-methyltetradecanoic acid (i-C15h3) and 3-hydroxy-12-methyltetradecanoic acid (a-C15h3).
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000037:antagonists & inhibitors*; D001412:Bacillus subtilis / Q000032:analysis*; D002849:Chromatography, Gas; D005227:Fatty Acids / Q000032:analysis; D008401:Gas Chromatography-Mass Spectrometry; D009682:Magnetic Resonance Spectroscopy; D008745:Methylation; D009842:Oligopeptides / Q000302:isolation & purification* / Q000494:pharmacology; D012988:Soil Microbiology
D005227:Fatty Acids; D009842:Oligopeptides; D015105:3',5'-Cyclic-AMP Phosphodiesterases