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ENZYMATIC FORMATION OF GLIDOBACTAMINE: A PEPTIDE NUCLEUS OF GLIDOBACTINS A, B AND C, NEW LIPOPEPTIDE ANTITUMOR ANTIBIOTICS

Glidobactin deacylating activity was found in a bacterial strain of Pseudomonas sp. Glidobactamine, a key intermediate for acyl analogues of glidobactin, was isolated from the enzymatic degradation products of glidobactins after treatment using a column of fibrous active gel on which the cells of th...

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Bibliographic Details
Published in:Journal of antibiotics 1988/10/25, Vol.41(10), pp.1351-1357
Main Authors: NUMATA, KEI-ICHI, OKA, MASAHISA, NAKAKITA, YASUKAZU, MURAKAMI, TSUTOMU, MIYAKI, TAKEO, KONISHI, MASATAKA, OKI, TOSHIKAZU, KAWAGUCHI, HIROSHI
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Language:English
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Summary:Glidobactin deacylating activity was found in a bacterial strain of Pseudomonas sp. Glidobactamine, a key intermediate for acyl analogues of glidobactin, was isolated from the enzymatic degradation products of glidobactins after treatment using a column of fibrous active gel on which the cells of the Pseudomonas strain were immobilized. The chemical structure of glidobactamine was confirmed as the intact peptide moiety of glidobactins by chemical reformation of glidobactin A from glidobactamine and 2, 4-dodecadienoic acid which is the constitutive fatty acid of glidobactin A.
ISSN:0021-8820
1881-1469
DOI:10.7164/antibiotics.41.1351