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A New Siderophore Isolated from Streptomyces sp. TM‐34 with Potent Inhibitory Activity Against Angiotensin‐Converting Enzyme
Author(s) -
Kodani Shinya,
OhnishiKameyama Mayumi,
Yoshida Mitsuru,
Ochi Kozo
Publication year - 2011
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.201100189
Subject(s) - siderophore , chemistry , streptomyces , enzyme , stereochemistry , inhibitory postsynaptic potential , enzyme inhibitor , strain (injury) , biochemistry , serine , biological activity , in vitro , bacteria , biology , genetics , neuroscience , gene , anatomy
Abstract A new siderophore named tsukubachelin was isolated from an iron‐deficient culture medium of newly isolated strain Streptomyces sp. TM‐34. The chemical structure of tsukubachelin was established by the interpretation of 2D NMR and TOF‐Mass spectroscopic data. The structure of tsukubachelin consists of six amino acid residues, including three serine, and one each of N ‐α‐methyl‐ N ‐δ‐hydroxy‐ N ‐δ‐formylornithine, N ‐α‐methyl‐ N ‐δ‐hydroxyornithine, and cyclic N ‐hydroxyornithine. Because the structurally related siderophore, desferri‐foroximithine, was reported to have potent angiotensin‐converting enzyme inhibition activity, the inhibitory activity of desferri‐tsukubachelin and desferri‐foroximithine were tested for structure–activity comparison. Desferri‐tsukubachelin showed 14 times more potent inhibitory activity than desferri‐foroximithine. This result indicates that desferri‐tsukubachelin may become a promising agent for angiotensin‐converting enzyme inhibition.