81276-27-9Relevant articles and documents
Efficient chemoenzymatic synthesis of novel galacto-N-biose derivatives and their sialylated forms
Li, Lei,Liu, Yonghui,Li, Tiehai,Wang, Wenjun,Yu, Zaikuan,Ma, Cheng,Qu, Jingyao,Zhao, Wei,Chen, Xi,Wang, Peng G.
, p. 10310 - 10313 (2015)
Galacto-N-biose (GNB) derivatives were efficiently synthesized from galactose derivatives via a one-pot two-enzyme system containing two promiscuous enzymes from Bifidobacterium infantis: a galactokinase (BiGalK) and a d-galactosyl-β1-3-N-acetyl-d-hexosamine phosphorylase (BiGalHexNAcP). Mono-sialyl and di-sialyl galacto-N-biose derivatives were then prepared using a one-pot two-enzyme system containing a CMP-sialic acid synthetase and an α2-3-sialyltransferase or an α2-6-sialyltransferase.
Studies on the substrate specificity of Escherichia coli galactokinase
Yang, Jie,Fu, Xun,Jia, Qiang,Shen, Jie,Biggins, John B.,Jiang, Jiqing,Zhao, Jingjing,Schmidt, Joshua J.,Wang, Peng G.,Thorson, Jon S.
, p. 2223 - 2226 (2007/10/03)
(Martix presented) In vitro glycorandomization (IVG) technology is dependent upon the ability to rapidly synthesize sugar phosphates. Compared with chemical synthesis, enzymatic (kinase) routes to sugar phosphates would be attractive for this application. This work focuses upon the development of a high-throughput colorimetric galactokinase (GalK) assay and its application toward probing the substrate specificity and kinetic parameters of Escherichia coli GalK. The demonstrated dinitrosalicylic assay should also be generally applicable to a variety of sugar-processing enzymes.
