38665-10-0Relevant articles and documents
Molecular basis for trehalase inhibition revealed by the structure of trehalase in complex with potent inhibitors
Gibson, Robert P.,Gloster, Tracey M.,Roberts, Shirley,Warren, R. Anthony J.,Storch De Gracia, Isabel,Garcia, Angela,Chiara, Jose L.,Davies, Gideon J.
, p. 4115 - 4119 (2007)
Strong inhibitions: The inhibition of trehalases, enzymes which hydrolyze the disaccharide trehalose, is a target for novel antibiotic insecticides. The structures (see picture; C black, N blue, O red, S yellow) of a trehalase in complex with validoxylami
Synthesis of [7-3H]valienamine, [7-3H]valienone, [7-3H]valiolamine and [7-3H]valiolone from validamycin A
Lee, Sungsook,Tornus, Ingo,Dong, Haijun,Groeger, Stefan
, p. 361 - 372 (2007/10/03)
To investigate the biosynthetic pathway to the cyclitol moieties of acarbose and validamycin A, [7-3H]valienamine, [7-3H]valienone, [7-3H]valiolamine and [7-3H]valiolone were synthesized as plausible precursors. Valienamine together with validamine was isolated from the degradation of validamycin A by Flavobacterium saccharophilum and served as starting material for the synthesis. Validamine was removed partially at the stage of tritylation and completely after the oxidation of the primary hydroxy group at C-7 to the aldehyde. The resulting valienamine aldehyde was reduced with tritiated sodium borohydride to produce [7-3H]valienamine. The latter was converted to [7-3H]valiolamine by a synthetic route described in the literature. The 3H-labeled amines were oxidized to [7-3H]valienone and [7-3H]valiolone, respectively, using 3,5-di-tert-butyl-1,2-bezoquinone (DBQ) followed by hydrolysis with oxalic acid.
Total Synthesis of (+)-Validoxylamine A
Ogawa, Seiichiro,Miyamoto, Yasunobu
, p. 889 - 890 (2007/10/02)
(+)-Validoxylamine A was synthesized by selective deoxygenation of (+)-validoxylamine B derivative, which was obtained by the coupling of the partially protected (+)-valienamine and (1R,2S,5R,7R,8R,9R,10R)-8,9-dibenzyloxy-5-phenyl-4,6,11-trioxatricyclo8.