Highly efficient chemoenzymatic synthesis of beta1-4-linked galactosides with promiscuous bacterial beta1-4-galactosyltransferases.
Two bacterial beta1-4-galactosyltransferases, NmLgtB and Hp1-4GalT, exhibit promiscuous and complementary acceptor substrate specificity. They have been used in an efficient one-pot multienzyme system to synthesize LacNAc, lactose, and their derivatives including those containing negatively charged 6-O-sulfated GlcNAc and C2-substituted GlcNAc or Glc, from monosaccharide derivatives and inexpensive Glc-1-P.
Lau
Kam
K
Department of Chemistry, University of California, One Shields Avenue, Davis, California 95616, USA.
Thon
Vireak
V
Yu
Hai
H
Ding
Li
L
Chen
Yi
Y
Muthana
Musleh M
MM
Wong
Denton
D
Huang
Ronald
R
Chen
Xi
X
D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D005697:Galactosides / Q000138:chemical synthesis* / Q000737:chemistry; D016480:Helicobacter pylori / Q000201:enzymology*; D009237:N-Acetyllactosamine Synthase / Q000737:chemistry* / Q000235:genetics; D009345:Neisseria meningitidis / Q000201:enzymology*; D016979:Pasteurella multocida / Q000201:enzymology*; D011993:Recombinant Fusion Proteins / Q000737:chemistry* / Q000235:genetics; D013379:Substrate Specificity
D005697:Galactosides; D011993:Recombinant Fusion Proteins; D009237:N-Acetyllactosamine Synthase