Abstract
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.
Recommended Citation
R. Mehra-Chaudhary et al., "In Crystallo Capture of a Covalent Intermediate in the UDP-Galactopyranose Mutase Reaction," Biochemistry, vol. 55, no. 6, pp. 833 - 836, American Chemical Society, Feb 2016.
The definitive version is available at https://doi.org/10.1021/acs.biochem.6b00035
Department(s)
Chemistry
Publication Status
Open Access
International Standard Serial Number (ISSN)
1520-4995; 0006-2960
Document Type
Article - Journal
Document Version
Citation
File Type
text
Language(s)
English
Rights
© 2024 American Chemical Society, All rights reserved.
Publication Date
16 Feb 2016
PubMed ID
26836146
Comments
U.S. Department of Energy, Grant DE-AC02-05CH11231