79902-99-1Relevant articles and documents
3-O-α-d-glucopyranosyl-L-rhamnose phosphorylase from Clostridium phytofermentans
Nihira, Takanori,Nakai, Hiroyuki,Kitaoka, Motomitsu
, p. 94 - 97 (2012)
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.
Synthesis of structural elements of the capsular polysaccharides of Streptococcus pneumoniae types 6A and 6B
Slaghek, Ted M.,Oijen, Anita H. van,Maas, Augustinus A. M.,Kamerling, Johannis P.,Vliegenthart, Johannes F. G.
, p. 237 - 248 (2007/10/02)
O-α-D-Glucopyranosyl-(1->3)-α,β-L-rhamnopyranose (15), O-α-D-galactopyranosyl-(1->3)-O-α-glucopyranosyl-(1->3)-α,β-L-rhamnopyranose (17), O-α-D-galactopyranosyl-(1->3)-O-α-D-glucopyranosyl-(1->3)-O-α-L-rhamnopyranosyl-(1->3)-D-ribitol (23), and O-α-D-gala