Cellobiose phosphorylase from Cellulomonas uda (CuCPase) is shown to utilize D-glucal as slow alternative donor substrate for stereospecific glycosyl transfer to inorganic phosphate, giving 2-deoxy-α-D-glucose 1-phosphate as the product. When performed in D(2)O, enzymatic phosphorolysis of D-glucal proceeds with incorporation
A total synthesis of the 12-membered ring natural macrolide, sporiolide B, was achieved from D-glucal in 17 steps with 4.8% overall yield. The required stereochemical configuration at C-3 and C-5 in sporiolide B was easily introduced by applying a Mitsunobu
Monoclonal antibodies (mAbs), 4H2 and 6H7, were prepared previously using a protein conjugate of a 1:1 epimeric mixture of the synthetic ABC-ring fragments of ciguatoxin (CTX), 3 and 4. Here, the interactions of these mAbs with the fragments of CTX
Alpha-Glucosidases from Aspergillus niger, pig serum, ungerminated rice, buckwheat, and sugar beet seeds (but not from brewers' yeast or honeybee) were found to catalyze the hydration of D-glucal. Each reactive alpha-glucosidase, incubated with D-glucal in D2O, was shown to protonate
The role of pyridoxal 5'-phosphate and orthophosphate in general acid-base catalysis by alpha-glucan phosphorylases.
H W Klein et al.
Progress in clinical and biological research, 144A, 147-160 (1984-01-01)
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