A unique flavin mononucleotide-linked primary alcohol oxidase for glycopeptide A40926 maturation

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

doi:10.1021/ja075748x

A unique flavin mononucleotide-linked primary alcohol oxidase for glycopeptide A40926 maturation

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^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

27 Citations (Scopus)

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.

Original language	English
Pages (from-to)	13384-13385
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	129
Issue number	44
DOIs	https://doi.org/10.1021/ja075748x
Publication status	Published - 7 Nov 2007
Externally published	Yes

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title = "A unique flavin mononucleotide-linked primary alcohol oxidase for glycopeptide A40926 maturation",

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.",

author = "Li, {Yi Shan} and Ho, {Jin Yuan} and Huang, {Chia Chi} and Lyu, {Syue Yi} and Lee, {Chun Yen} and Huang, {Yu Ting} and Wu, {Chang Jer} and Chan, {Hsiu Chien} and Huang, {Chuan Jiuan} and Hsu, {Ning Shian} and Tsai, {Ming Daw} and Li, {Tsung Lin}",

year = "2007",

month = nov,

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doi = "10.1021/ja075748x",

language = "English",

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pages = "13384--13385",

journal = "Journal of the American Chemical Society",

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T1 - A unique flavin mononucleotide-linked primary alcohol oxidase for glycopeptide A40926 maturation

AU - Li, Yi Shan

AU - Ho, Jin Yuan

AU - Huang, Chia Chi

AU - Lyu, Syue Yi

AU - Lee, Chun Yen

AU - Huang, Yu Ting

AU - Wu, Chang Jer

AU - Chan, Hsiu Chien

AU - Huang, Chuan Jiuan

AU - Hsu, Ning Shian

AU - Tsai, Ming Daw

AU - Li, Tsung Lin

PY - 2007/11/7

Y1 - 2007/11/7

N2 - 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.

AB - 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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U2 - 10.1021/ja075748x

DO - 10.1021/ja075748x

M3 - Article

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AN - SCOPUS:35948952728

SN - 0002-7863

VL - 129

SP - 13384

EP - 13385

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 44

ER -

A unique flavin mononucleotide-linked primary alcohol oxidase for glycopeptide A40926 maturation

Abstract

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