An enzymatic tandem reaction is described in which the enzymes phosphorylase and Deinococcus geothermalis glycogen branching enzyme (Dg GBE) catalyze the synthesis of branched polyglucans from glucose‐1‐phosphate (G‐1‐P). Phosphorylase consumes G‐1‐P and polymerizes linear amylose while Dg GBE introduces branching points on the α ‐(1 → 6) positions by reshuffling short oligosaccharides. The resulting branched polyglucans have an unusually high degree of branching of 11%.
Glycoside hydrolase family 57 glycogen branching enzymes (GH57GBE)
catalyze the formation of an α-1,6 glycosidic bond between α-1,4 linked
glucooliogosaccharides. As an atypical family, a limited number of
GH57GBEs have been biochemically characterized so far. This study aimed
at acquiring a better understanding of the GH57GBE family by a
systematic sequence-based bioinformatics analysis of almost 2,500 gene
sequences and determining the branching activity of several native and
mutant GH57GBEs. A correlation was found between a very low or even no
branching activity with the absence of a flexible loop, a tyrosine at
the loop tip, and two β-sheets.
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