The Journal of Antibiotics
Online ISSN : 1881-1469
Print ISSN : 0021-8820
ISSN-L : 0021-8820
ACYLPEPTIDES, THE INHIBITORS OF CYCLIC ADENOSINE 3', 5'-MONOPHOSPHATE PHOSPHODIESTERASE
I. PURIFICATION, PHYSICOCHEMICAL PROPERTIES AND STRUCTURES OF FATTY ACID RESIDUES
KUNIAKI HOSONOHIDEO SUZUKI
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1983 Volume 36 Issue 6 Pages 667-673

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Abstract

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 β-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 (α-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 (α-C15h3).

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