Premium
Mechanistic Implications of Escherichia coli Galactokinase Structure‐Based Engineering
Author(s) -
Hoffmeister Dirk,
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.200400003
Subject(s) - galactokinase , escherichia coli , stacking , substrate (aquarium) , protein engineering , chemistry , active site , galactose , hydrogen bond , biochemistry , stereochemistry , biology , enzyme , organic chemistry , molecule , ecology , gene
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.