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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/27135

Title: A Unique Flavin Mononucleotide-Linked Primary Alcohol Oxidase for Glycopeptide A40926 Maturation
Authors: Yi-Shan Li;Jin-Yuan Ho;Chia-Chi Huang;Syue-Yi Lyu;Chun-Yen Lee;Yu-Ting Huang;Chang-Jer Wu;Hsiu-Chien Chan;Chuan-Jiuan Huang;Ning-Shian Hsu;Ming-Daw Tsai;Tsung-Lin Li
Contributors: NTOU:Department of Food Science
Date: 2007
Issue Date: 2011-10-21T02:23:41Z
Publisher: Journal of the American Chemical Society
Abstract: 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.
Relation: 129(44), pp.13384–13385
URI: http://ntour.ntou.edu.tw/handle/987654321/27135
Appears in Collections:[食品科學系] 期刊論文

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