Mechanistic implications of Escherichia coli galactokinase structure-based engineering

被引：24

作者：

Hoffmeister, D ^{[1
]}

Thorson, JS ^{[1
]}

机构：

[1] Univ Wisconsin, Sch Pharm, Lab Biosynthet Chem, Madison, WI 53705 USA

来源：

CHEMBIOCHEM | 2004年 / 5卷 / 07期

关键词：

carbohydrates; enzymes; glycorandomization; kinases; phosphosugars;

D O I：

10.1002/cbic.200400003

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Engineering GalK: The Escherichia coli galactokinase GalK has been engineered in its active site. The amino acid exchanges Y223F and Y223W broadened the sugar-substrate spectrum to include, among others, 4-deoxy-D-galactose. This finding suggests that the role of Y223 is not primarily hydrogen bonding but rather a hydrophobic stacking to secure the hexopyranose ring in the active site.

引用

页码：989 / 992

页数：4

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