Efficient chemoenzymatic synthesis of globotriose and its derivatives with a recombinant alpha-(1-->4)-galactosyltransferase.
A truncated alpha-(1-->4)-galactosyltransferase (LgtC) gene from Neisseria meningitidis was cloned. The recombinant glycosyltransferase was expressed in Escherichia coli BL21 (DE3) strain with high specific activity (5 units/mg protein). Its acceptor specificity was carefully characterized. Then the purified enzyme was utilized in highly efficient syntheses of globotriose and a variety of alpha-(1-->4)-galactosylated derivatives as potential antibacterial agents.
Zhang
Jianbo
J
Department of Chemistry, Wayne State University, Detroit, MI 48202, USA.
Kowal
Przemyslaw
P
Fang
Jianwen
J
Andreana
Peter
P
Wang
Peng George
PG
D001426:Bacterial Proteins / Q000378:metabolism; D002240:Carbohydrate Sequence; D003001:Cloning, Molecular; D016695:Glycosyltransferases / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009345:Neisseria meningitidis / Q000378:metabolism; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity; D014312:Trisaccharides / Q000138:chemical synthesis* / Q000737:chemistry
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D014312:Trisaccharides; C113460:globotriose; D016695:Glycosyltransferases; C101829:LgtC protein, Neisseria