Title : Preparative and Kinetic Analysis of β-1,4- and β-1,3-Glucan Phosphorylases Informs Access to Human Milk Oligosaccharide Fragments and Analogues Thereof.

Pub. Date : 2020 Apr 1

PMID : 31657512






2 Functional Relationships(s)
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1 Without recourse to enzyme engineering or evolution approaches, here we demonstrate the ability of wild-type cellodextrin phosphorylase (CDP: beta-1,4-glucan linkage-dependent) and laminaridextrin phosphorylase (Pro_7066: beta-1,3-glucan linkage-dependent) to tolerate a number of sugar-1- phosphate substrates, albeit with reduced kinetic efficiency. Cytidine Diphosphate UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens
2 Without recourse to enzyme engineering or evolution approaches, here we demonstrate the ability of wild-type cellodextrin phosphorylase (CDP: beta-1,4-glucan linkage-dependent) and laminaridextrin phosphorylase (Pro_7066: beta-1,3-glucan linkage-dependent) to tolerate a number of sugar-1- phosphate substrates, albeit with reduced kinetic efficiency. Cytidine Diphosphate UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens