The structures of katanosins A and B.
1H and 13C NMR studies on katanosin A confirmed the presence of eight usual amino acid residues which were previously deduced by amino acid analysis and suggested the presence of beta-hydroxyaspartic acid, beta-hydroxyleucine and beta-phenylserine residues. These amino acids were isolated and confirmed, including their stereochemistries, by comparison with the respective authentic specimens. Stereochemistries of the usual amino acids were determined by comparing the L-leucylated amino acids with reference compounds by HPLC. Lithium borohydride reduction and chromic acid oxidation of katanosin A and alkali-treated katanosin A elucidated a lactone linkage between the C-terminal Ser and phenylserine residues. Edman degradation on alkali-treated katanosin A clarified the total amino acid sequence. The difference in katanosins A and B was determined to be replacement of Val in A by Ile in B. Thus, the structures of katanosins A and B were elucidated.
Kato
T
T
Shionogi Research Laboratories, Shionogi & Co., Ltd., Osaka, Japan.
Hinoo
H
H
Terui
Y
Y
Kikuchi
J
J
Shoji
J
J
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000900:Anti-Bacterial Agents / Q000032:analysis*; D055598:Chemical Phenomena; D002621:Chemistry; D047630:Depsipeptides; D010455:Peptides / Q000032:analysis
D000596:Amino Acids; D000900:Anti-Bacterial Agents; D047630:Depsipeptides; D010455:Peptides; C056789:katanosin A; C056790:katanosin B