114779-32-7Relevant articles and documents
Pseudoglycosyltransferase catalyzes nonglycosidic C-N coupling in validamycin a biosynthesis
Asamizu, Shumpei,Yang, Jongtae,Almabruk, Khaled H.,Mahmud, Taifo
experimental part, p. 12124 - 12135 (2011/10/09)
Glycosyltransferases are ubiquitous in nature. They catalyze a glycosidic bond formation between sugar donors and sugar or nonsugar acceptors to produce oligo/polysaccharides, glycoproteins, glycolipids, glycosylated natural products, and other sugar-containing entities. However, a trehalose 6-phosphate synthase-like protein has been found to catalyze an unprecedented nonglycosidic C-N bond formation in the biosynthesis of the aminocyclitol antibiotic validamycin A. This dedicated 'pseudoglycosyltransferase catalyzes a condensation between GDP-valienol and validamine 7-phosphate to give validoxylamine A 7′-phosphate with net retention of the 'anomeric configuration of the donor cyclitol in the product. The enzyme operates in sequence with a phosphatase, which dephosphorylates validoxylamine A 7′-phosphate to validoxylamine A.
Synthesis of valiolamine and its N-substituted derivatives AO-128, validoxylamine G, and validamycin G via branched-chain inosose derivatives
Fukase,Horii
, p. 3651 - 3658 (2007/10/02)
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STEREOCONTROLLED SYNTHESIS OF (+)-VALIENAMINE
Nicotra, Francesco,Panza, Luigi,Ronchetti, Fiamma,Russo, Giovanni
, p. 577 - 580 (2007/10/02)
(+)-Valienamine, 1, constituent of antibiotics and α-glucosidase inhibitors, is synthesized through a simple and stereoselective procedure, starting from the easily available enone 3.A stereoselective access to 6-epivalienamine, 2, from the same precursor is also described.