24960-12-1Relevant academic research and scientific papers
Mechanistic studies of the radical S-adenosylmethionine enzyme DesII with TDP-D-fucose
Ko, Yeonjin,Ruszczycky, Mark W.,Choi, Sei-Hyun,Liu, Hung-Wen
, p. 860 - 863 (2015/03/05)
DesII is a radical S-adenosylmethionine (SAM) enzyme that catalyzes the C4-deamination of TDP-4-amino-4,6-dideoxyglucose through a C3 radical intermediate. However, if the C4 amino group is replaced with a hydroxy group (to give TDP-quinovose), the hydroxy group at C3 is oxidized to a ketone with no C4-dehydration. It is hypothesized that hyperconjugation between the C4 C-N/O bond and the partially filled p orbital at C3 of the radical intermediate modulates the degree to which elimination competes with dehydrogenation. To investigate this hypothesis, the reaction of DesII with the C4-epimer of TDP-quinovose (TDP-fucose) was examined. The reaction primarily results in the formation of TDP-6-deoxygulose and likely regeneration of TDP-fucose. The remainder of the substrate radical partitions roughly equally between C3-dehydrogenation and C4-dehydration. Thus, changing the stereochemistry at C4 permits a more balanced competition between elimination and dehydrogenation.
dTDP-BETA-D-FUCOFURANOSE, ITS PREPARATION METHOD AND USE
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Page/Page column 4, (2012/03/08)
Provided is a dTDP-β-D-fucofuranose, which is also referred to as dTDP-β-6-deoxy-D-galactofuranose. The dTDP-β-D-fucofuranose is synthesized by using reductase Fcf1 and mutase Fcf2 in the gram-negative bacteria. Also provided are the preparation method of the dTDP-β-D-fucofuranose and use of the dTDP-β-D-fucofuranose for manufacturing a medicament for the treatment of tumors.
