Characterisation of a Bacterial Galactokinase with High Activity and Broad Substrate Tolerance for Chemoenzymatic Synthesis of 6-Aminogalactose-1-Phosphate and Analogues
作者:Kun Huang、Fabio Parmeggiani、Edward Pallister、Chuen-Jiuan Huang、Fang-Fang Liu、Qian Li、William R. Birmingham、Peter Both、Baptiste Thomas、Li Liu、Josef Voglmeir、Sabine L. Flitsch
DOI:10.1002/cbic.201700477
日期:2018.2.16
Furnishing phosphates: A galactokinase from L. grimontii (LgGalK) has been identified and characterised; it shows broad substrate specificity towards different nucleotide phosphates and monosaccharides. This enzyme, in combination with a galactose oxidase variant was used in the chemoenzymatic synthesis of a panel of 6‐aminogalactose‐1‐phosphateanalogues.
Promiscuous galactokinases (GalKs), which catalyse the ATP dependent phosphorylation of galactose in nature, have been widely exploited in biotechnology for the rapid synthesis of diverse sugar-1-phosphates. This work focuses on the characterisation of a bacterial GalK from Streptomyces coelicolor (ScGalK), which was overproduced in Escherichia coli and shown to phosphorylate galactose. ScGalK displayed