The structure of M-GTFI, an inhibitor of glucosyltransferase from S. mutans, and its inhibitory relationship with other sulfate ester-containing inhibitors

• Published in: Journal of enzyme inhibition Vol. 2; no. 4; p. 279
• Main Authors: Uyeda, M, Oshima, H, Nishi, K, Suzuki, K, Yahara, S, Nohara, T, Shibata, M
• Format: Journal Article
• Language: English
• Published: Switzerland 1989
• Subjects: Alkanesulfonates - isolation & purification; Alkanesulfonates - pharmacology; Glucosyltransferases - antagonists & inhibitors; Hydrolysis; Lactones - isolation & purification; Lactones - pharmacology; Magnetic Resonance Spectroscopy; Mass Spectrometry; Micromonospora; Spectrophotometry, Infrared; Streptococcus mutans - enzymology
• ISSN: 8755-5093
• DOI: 10.3109/14756368909088481

M-GTFI, an inhibitor of glucosyltransferase from S. mutans was produced by Micromonospora narashinoensis strain No. 731. The isolation procedure for M-GTFI was improved and established for spectroscopic analyses, and some properties of the inhibitor were investigated. The structure of M-GTFI was shown to be trisodium [2-sulphonato-(E)-9-undecenyll-oxacyclotriacont-(E)-3- en-2-one, 16, 18-bis sulphonate. The chemical structure of M-GTFI was therefore similar to that of izumenolide which is a beta-lactamase inhibitor containing sulfate ester groups in its molecule. The inhibitory characteristics of M-GTFI were parallel to that of other inhibitory compounds containing sulphate esters but the spectrum of activity was wider.