A Unique Flavin Mononucleotide-Linked Primary Alcohol Oxidase for Glycopeptide A40926 Maturation | Zendy

Yishan Li | Zendy; JinYuan Ho | Zendy; Chia-Chi Flora Huang | Zendy; SyueYi Lyu | Zendy; Chun-Yen Lee | Zendy; YuTing Huang | Zendy; ChangJer Wu | Zendy; HsiuChien Chan | Zendy; ChuenJiuan Huang | Zendy; NingShian Hsu | Zendy; MingDaw Tsai | Zendy; TsungLin Li | Zendy

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A Unique Flavin Mononucleotide-Linked Primary Alcohol Oxidase for Glycopeptide A40926 Maturation

Author(s) -

Yishan Li,

JinYuan Ho,

Chia-Chi Flora Huang,

SyueYi Lyu,

Chun-Yen Lee,

YuTing Huang,

ChangJer Wu,

HsiuChien Chan,

ChuenJiuan Huang,

NingShian Hsu,

MingDaw Tsai,

TsungLin Li

Publication year - 2007

Publication title -

journal of the american chemical society

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 7.115

H-Index - 612

eISSN - 1520-5126

pISSN - 0002-7863

DOI - 10.1021/ja075748x

Subject(s) - chemistry , flavin mononucleotide , glycopeptide , biochemistry , flavin group , enzyme , biosynthesis , stereochemistry , antibiotics

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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