Abstract
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.
Original language | English |
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Pages (from-to) | 992-996 |
Number of pages | 5 |
Journal | ChemBioChem |
Volume | 5 |
Issue number | 7 |
DOIs | |
State | Published - Jul 5 2004 |
Keywords
- Glucose
- Kinases
- Mutagenesis
- Protein design
- Sugars
ASJC Scopus subject areas
- Biochemistry
- Molecular Medicine
- Molecular Biology
- Organic Chemistry