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 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.
D000903:Antibiotics, Antineoplastic / Q000096:biosynthesis / Q000302:isolation & purification* / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D002855:Chromatography, Thin Layer; D008239:Lysine / Q000031:analogs & derivatives / Q000378:metabolism; D010456:Peptides, Cyclic; D011549:Pseudomonas / Q000302:isolation & purification / Q000378:metabolism; D013912:Threonine / Q000031:analogs & derivatives* / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism
D000903:Antibiotics, Antineoplastic; D010456:Peptides, Cyclic; C057881:glidobactamine; C057878:glidobactin A; C057879:glidobactin B; C057880:glidobactin C; D013912:Threonine; D008239:Lysine