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CDA: Calcium‐Dependent Peptide Antibiotics from Streptomyces coelicolor A3(2) Containing Unusual Residues
Author(s) -
Kempter Christoph,
Kaiser Dietmar,
Haag Sabine,
Nicholson Graeme,
Gnau Volker,
Walk Tilmann,
Gierling Karl Heinz,
Decker Heinrich,
Zähner Hans,
Jung Günther,
Metzger Jörg W.
Publication year - 1997
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199704981
Subject(s) - streptomyces coelicolor , chemistry , peptide , mass spectrometry , calcium , antibiotics , stereochemistry , streptomycetaceae , actinomycetales , streptomyces , biochemistry , crystallography , bacteria , organic chemistry , chromatography , biology , mutant , gene , genetics
Only in the presence of Ca 2+ are ions channels formed by peptides of the group of calcium‐dependent antibiotics (CDA). O‐Phosphorylated D ‐3‐hydroxyasparagine is one of the unusual residues in the microheterogeneous CDA undecapeptide lactone isolated from Streptomyces coelicolor A3(2) (see below). By combination of modern analytical methods, such as the coupling of a gas‐phase sequencer to a mass spectrometer, a total of four structures could be elucidated from only a few milligrams of product.