Efficient chemoenzymatic synthesis of globotriose and its derivatives with a recombinant alpha-(1-->4)-galactosyltransferase

Jianbo Zhang; Przemyslaw Kowal; Jianwen Fang; Peter Andreana; Peng George Wang

doi:10.1016/s0008-6215(02)00106-4

Efficient chemoenzymatic synthesis of globotriose and its derivatives with a recombinant alpha-(1-->4)-galactosyltransferase

Carbohydr Res. 2002 Jun 5;337(11):969-76. doi: 10.1016/s0008-6215(02)00106-4.

Authors

Jianbo Zhang¹, Przemyslaw Kowal, Jianwen Fang, Peter Andreana, Peng George Wang

Affiliation

¹ Department of Chemistry, Wayne State University, Detroit, MI 48202, USA.

PMID: 12039536
DOI: 10.1016/s0008-6215(02)00106-4

Abstract

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.

MeSH terms

Bacterial Proteins / metabolism
Carbohydrate Sequence
Cloning, Molecular
Glycosyltransferases / genetics
Glycosyltransferases / metabolism*
Molecular Sequence Data
Neisseria meningitidis / metabolism
Recombinant Proteins / genetics
Recombinant Proteins / metabolism
Substrate Specificity
Trisaccharides / chemical synthesis*
Trisaccharides / chemistry

Substances

Bacterial Proteins
Recombinant Proteins
Trisaccharides
globotriose
Glycosyltransferases
LgtC protein, Neisseria