Structures of cepafungins I, II and III.
Structures of interesting acylpeptide antibiotics cepafungins I, II and III were elucidated by NMR spectroscopic studies and some degradation experiments. The antibiotics contain a common peptide part that consists of threonine and two unusual amino acid residues, gamma-hydroxylysine and 4-amino-2-pentenoic acid. The unusual amino acid residues compose an interesting 12-membered ring with an exocyclic N-terminus to which the threonine is connected. Different fatty acyl groups connected to the N-terminus of the threonine distinguish the three cepafungins. The major component I and minor component III are new substance, but the minor component II has a structure identical with that of the recently reported antibiotic glidobactin A.
Terui
Y
Y
Shionogi Research Laboratories, Shionogi & Co., Ltd. Osaka, Japan.
Nishikawa
J
J
Hinoo
H
H
Kato
T
T
Shoji
J
J
D000596:Amino Acids / Q000032:analysis; D000903:Antibiotics, Antineoplastic / Q000032:analysis*; D000935:Antifungal Agents / Q000032:analysis*; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D008968:Molecular Conformation; D015394:Molecular Structure; D010456:Peptides, Cyclic / Q000032:analysis
D000596:Amino Acids; D000903:Antibiotics, Antineoplastic; D000935:Antifungal Agents; D010456:Peptides, Cyclic; C057878:glidobactin A; C065441:cepafungin I; C065443:cepafungin III