A Unique Flavin Mononucleotide-Linked Primary Alcohol Oxidase for Glycopeptide A40926 Maturation
Resource
Journal of the American Chemical Society 129 (44): 13384-13385
Journal
Journal of the American Chemical Society
Pages
13384-13385
Date Issued
2007
Date
2007
Author(s)
Li, Yi-Shan
Ho, Jin-Yuan
Huang, Chia-Chi
Lyu, Syue-Yi
Lee, Chun-Yen
Huang, Yu-Ting
Wu, Chang-Jer
Chan, Hsiu-Chien
Huang, Chuan-Jiuan
Hsu, Ning-Shian
Tsai, Ming-Daw
Li, Tsung-Lin
Abstract
The unique pharmacokinetic and pharmacodynamic activities of glycopeptide antibiotics are conferred by tailoring steps occurring on the aglycone. Here, we report that protein Dbv29, involved in the biosynthesis of A40926, is a novel flavin mononucleotide-dependent primary alcohol glycopeptide hexose oxidase that carries out a four-electron oxidation reaction. Dbv29 catalyzes the last step in a multistep sequence to complete N-acyl aminoglucuronic acid substituent biosynthesis for a potent drug lead. The characterized enzyme may provide a new way to enhance the efficacy of currently used glycopeptide drugs. This detailed function-mechanism analysis of the enzyme increases our knowledge of this new class of enzyme.
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