title: Enzymatic synthesis of alpha-anomer-selective D-glucosides using maltose phosphorylase.
abstract: A maltose phosphorylase (EC 2.4.1.8; MPase) showed novel acceptor specificity and transferred the glucosyl moiety of maltose not only to sugars but also to various acceptors having alcoholic OH groups. Salicyl alcohol acted as acceptor for MPase from Enterococcus hirae, and the product, salicyl-O-alpha-D-glucopyranoside (alpha-SalGlc) was identified. The yield based on supplied salicyl alcohol was 86% (mol/mol).
authors.affiliation: Department of Applied Chemistry, School of Science and Engineering, Waseda University, Japan. kkino@waseda.jp
authors.forename: Kuniki
authors.initials: K
authors.lastname: Kino
authors.forename: Yu
authors.initials: Y
authors.lastname: Shimizu
authors.forename: Shoko
authors.initials: S
authors.lastname: Kuratsu
authors.forename: Kohtaro
authors.initials: K
authors.lastname: Kirimura
mesh_terms: D001592:Benzyl Alcohols / Q000378:metabolism; D016983:Enterococcus / Q000201:enzymology; D005947:Glucose / Q000378:metabolism; D005960:Glucosides / Q000138:chemical synthesis*; D005964:Glucosyltransferases / Q000378:metabolism*; D008320:Maltose / Q000378:metabolism
chemical_list: D001592:Benzyl Alcohols; D005960:Glucosides; D008320:Maltose; D005964:Glucosyltransferases; C021535:maltose phosphorylase; C010631:salicyl alcohol; D005947:Glucose