New alpha-amylase inhibitor, trestatins. I. Isolation, characterization and biological activities of trestatins A, B and C.
Trestatin complex which exhibited a potent inhibitory activity on various alpha-amylases has been isolated from the culture filtrate of Streptomyces dimorphogenes nov. sp. NR-320-OM7HB. Three major components, trestatins A, B and C, have been purified by adsorption and ion-exchange chromatography. Their spectral and chemical properties suggested that trestatins were novel basic oligosaccharide homologues each characterized by the possession of a trehalose moiety at the non-reducing end of the molecule.
D002851:Chromatography, High Pressure Liquid; D009682:Magnetic Resonance Spectroscopy; D009844:Oligosaccharides / Q000302:isolation & purification*; D013055:Spectrophotometry, Infrared; D013302:Streptomyces / Q000254:growth & development*; D013329:Structure-Activity Relationship; D014312:Trisaccharides / Q000302:isolation & purification* / Q000494:pharmacology; D000516:alpha-Amylases / Q000037:antagonists & inhibitors*
D009844:Oligosaccharides; D014312:Trisaccharides; C038505:trestatin; D000516:alpha-Amylases