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Structure‐Based Enhancement of the First Anomeric Glucokinase
Author(s) -
Yang Jie,
Liu Lesley,
Thorson Jon S.
Publication year - 2004
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200400041
Subject(s) - galactokinase , glucokinase , biochemistry , chemistry , anomer , glycome , monosaccharide , glycosylation , enzyme , combinatorial chemistry , glycan , glycoprotein , escherichia coli , gene
Promoting promiscuity. The availability of D ‐glucose‐1‐phosphate and its derivatives directly contributes to the efficiency of in vitro and in vivo glycosylation methodologies, such as natural‐product glycorandomization. While one‐step enzymatic routes to this vital class of sugar phosphates provide an attractive alternative to multistep chemical syntheses, no sugar kinase studied thus far is known to anomerically phosphorylate D ‐glucose. Herein we report both the discovery of inherent glucokinase (GlcK) activity in wild‐type Lactococcus lactis galactokinase and the enhancement of this first GlcK to provide a catalyst capable of accepting a wide range of new monosaccharide substrates.