The structures of katanosins A and B.
- 1 January 1988
- journal article
- research article
- Published by Japan Antibiotics Research Association in The Journal of Antibiotics
- Vol. 41 (6) , 719-725
- https://doi.org/10.7164/antibiotics.41.719
Abstract
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.This publication has 3 references indexed in Scilit:
- Isolation and characterization of katanosins A and B.The Journal of Antibiotics, 1988
- The Non-Protein Amino AcidsPublished by Springer Nature ,1985
- Quantitative determination of D- and L-amino acids by reaction with tert-butyloxycarbonyl-L-leucine N-hydroxysuccinimide ester and chromatographic separation as L,D and L,L dipeptidesAnalytical Chemistry, 1978