94801-02-2Relevant articles and documents
Nickel(II)-catalysed transformations of 5-azido-5-deoxy-D-glucofuranose and of 5-azido-5-deoxy-L-idofuranose
Hadwiger, Philipp,Lechner, Andreas,Stuetz, Arnold E.
, p. 241 - 247 (1998)
Nickel(II) catalysed isomerisation reactions of C-5 modified derivatives of D-glucose as well as L-idose were investigated. 5-Azido-5-deoxy-D-glucofuranose was successfully isomerised into the corresponding D-manno epimer in good yields. Contrasting this result, in the case of the 5-modified L-idofuranose probed, no evidence for successful epimerisation at C-2 could be found. However, this sugar was quantitatively rearranged into the corresponding L-sorbopyranose. Upon extended reaction periods, the latter underwent degradation to give the coresponding 4-modified methyl L-xylonate.
2,5-Dideoxy-2,5-imino-D-mannitol and -D-glucitol. Two-step bio-organic syntheses from 5-azido-5-deoxy-D-glucofuranose and -L-idofuranose; evaluation as glucosidase inhibitors and application in affinity purification and characterisation of invertase from yeast
Legler,Korth,Berger,Ekhart,Gradnig,Stutz
, p. 67 - 77 (2007/10/02)
Glucose isomerase (EC 5.3.1.5) catalyzes the quantitative isomerisation of 5-azido-5-deoxy-D-gluco- (7) and -L-idofuranose (9), respectively, into the corresponding ketoses, 5-azido-5-deoxy-D-fructopyranose (8) and -L-sorbopyranose (10), respectively. Upon catalytic hydrogenation over palladium-on-charcoal, the fructose derivative 8 gives the natural product and the efficient glycosidase inhibitor 2,5-dideoxy-2,5-imino-D-mannitol (4), while the sorbose derivative 10 affords 2,5-dideoxy-2,5-imino-D-glucitol (5). This represents a preparatively very simple and efficient two-step synthesis of these biologically active compounds. Both are strong inhibitors of α- and β-glucosidases from various sources, the D-manno-isomer 4 being distinctly more active. Because of its structural relationship with β-D-fructofuranose, compound 4 is also a vary good inhibitor of invertase from yeast and, as such, was for the first time employed, after immobilized and aminohexyl-sepharose, for the purification of this enzyme. Glucose isomerase (EC 5.3.1.5) catalyses the quantitative isomerization of 5-azido-5-deoxy-D-gluco (7) and -L-idofuranose (9), respectively, into the corresponding ketoses, 5-azido-5-deoxy-D-fructopyranose (8) and -L-sorbopyranose (10) respectively. Upon catalytic hydrogenation over palladium on 2,5-dideoxy-2,5-imino-D-mannitol (4), while the sorbose derivative 10 affords 2,5-dideoxy-2,5-imino-D-glucitol (5). This represents a preparatively very simple and efficient two-step synthesis of these biologically active compounds. Both are strong inhibitors of α- and β-glucosidases from various sources, the D-manno-isomer 4 being distinctly more active. Because of its structural relationship with β-D-fructofuranose, compound 4 is also a very good inhibitor of invertase from yeast and, as such, was for the first time employed, after immobilization on aminohexyl-sepharose, for the purification of this enzyme.
α-Amino aldehyde equivalents as substrates for rabbit muscle aldolase: Synthesis of 1,4-dideoxy-D-arabinitol and 2(R),5(R)-bis (hydroxymethyl)-3(R),4(R)-dihydroxypyrrolidine
Hung,Straub,Whitesides
, p. 3849 - 3855 (2007/10/02)
-
