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Carbohydr Res. 2012 Mar 1;350:94-7. doi: 10.1016/j.carres.2011.12.019. Epub 2011 Dec 29.

3-O-α-D-glucopyranosyl-L-rhamnose phosphorylase from Clostridium phytofermentans.

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  • 1Faculty of Agriculture, Niigata University, Niigata, Japan.

Abstract

We found an unreported activity of phosphorylase catalyzed by a protein (Cphy1019) belonging to glycoside hydrolase family 65 (GH65) from Clostridium phytofermentans. The recombinant Cphy1019 produced in Escherichia coli did not phosphorolyze α-linked glucobioses, such as trehalose (α1-α1), kojibiose (α1-2), nigerose (α1-3), and maltose (α1-4), which are typical substrates for GH65 enzymes. In reverse phosphorolysis, Cphy1019 utilized only l-rhamnose as the acceptor among various sugars examined with β-d-glucose 1-phosphate as the donor. The reaction product was determined to be 3-O-α-d-glucopyranosyl-l-rhamnose, indicating strict α1-3 regioselectivity. We propose 3-O-α-d-glucopyranosyl-l-rhamnose: phosphate β-d-glucosyltransferase as the systematic name and 3-O-α-d-glucopyranosyl-l-rhamnose phosphorylase as the short name for this novel GH65 phosphorylase.

Copyright © 2011 Elsevier Ltd. All rights reserved.

PMID:
22277537
[PubMed - indexed for MEDLINE]
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