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The constituent fatty acid of cerexin A was elucidated to be beta-hydroxy isoundecanoic acid by gas chromatography, mass spectrometry and nuclear magnetic resonance. The asparaginyl asparagine linkage in the amino acid sequence of the antibiotic, which has been previously described, was proved to be a normal alpha-carboxylpeptide bond by dehydration-reduction procedure. The three asparagine residues in the sequence were isolated separately and their chiralities were determined. The structure of cerexin A was concluded from the above results.

The total structure of cerexin A. Studies on antibiotics from the genus Bacillus. XVI.