Enzymatic synthesis of alpha-anomer-selective D-glucosides using maltose phosphorylase.
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).
Kino
Kuniki
K
Department of Applied Chemistry, School of Science and Engineering, Waseda University, Japan. kkino@waseda.jp
Shimizu
Yu
Y
Kuratsu
Shoko
S
Kirimura
Kohtaro
K
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
D001592:Benzyl Alcohols; D005960:Glucosides; D008320:Maltose; D005964:Glucosyltransferases; C021535:maltose phosphorylase; C010631:salicyl alcohol; D005947:Glucose