In Crystallo Capture of a Covalent Intermediate in the UDP-Galactopyranose Mutase Reaction | Zendy

Ritcha MehraChaudhary | Zendy; Yumin Dai | Zendy; Pablo Sobrado | Zendy; John J. Tanner | Zendy

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In Crystallo Capture of a Covalent Intermediate in the UDP-Galactopyranose Mutase Reaction

Author(s) -

Ritcha MehraChaudhary,

Yumin Dai,

Pablo Sobrado,

John J. Tanner

Publication year - 2016

Publication title -

biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.43

H-Index - 253

eISSN - 1520-4995

pISSN - 0006-2960

DOI - 10.1021/acs.biochem.6b00035

Subject(s) - mutase , covalent bond , chemistry , flavin group , active site , stereochemistry , flavin mononucleotide , nucleophile , anomer , catalysis , enzyme , biochemistry , organic chemistry

UDP-galactopyranose mutase (UGM) plays an essential role in galactofuranose biosynthesis in pathogens by catalyzing the conversion of UDP-galactopyranose to UDP-galactofuranose. Here we report the first crystal structure of a covalent intermediate in the UGM reaction. The 2.3 Å resolution structure reveals UDP bound in the active site and galactopyranose linked to the FAD through a covalent bond between the anomeric C of galactopyranose and N5 of the FAD. The structure confirms the role of the flavin as nucleophile and supports the hypothesis that the proton destined for O5 of galactofuranose is shuttled from N5 of the FAD via O4 of the FAD.

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