Recent advances in the study of macrolide glycosyltransferases.
- Author:
Dong-Mei LIANG
1
;
Jian-Jun QIAO
Author Information
1. Department of Pharmaceutical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China.
- Publication Type:Journal Article
- MeSH:
Anti-Bacterial Agents;
metabolism;
pharmacology;
Drug Resistance, Bacterial;
Glucosyltransferases;
classification;
metabolism;
Glycosylation;
Macrolides;
chemistry;
metabolism;
Streptomyces;
enzymology;
Substrate Specificity
- From:
Acta Pharmaceutica Sinica
2007;42(5):455-462
- CountryChina
- Language:Chinese
-
Abstract:
Catalyzed by a family of enzymes called glycosyltransferases (GTases), glycosylation reactions are essential for the bioactivities of macrolide antibiotics which have been widely applied. Additionally, glycosylation is also an important strategy of microbial to get macrolide antibiotic resistance. Studies on the structure, function and application areas of macrolide GTases will lay the stable groundwork for the combinatorial biology. This paper introduced in detail the biological functions of macrolide glycosylation, and then made an in-depth discussion on the families and discoveries of macrolide GTases. The resistance mechanism with macrolide glycosyltion and the correlative GTases MGT have been reviewed afterwards. According to the flexible substrate specificity of macrolide GTases, the combinatorial biological applications on them were also seriously summarized here. At the end, the authors made a developmental prospect of macrolide GTases based on the studies of the research group.
