X-ray crystallography reveals a reduced substrate complex of UDP-galactopyranose mutase poised for covalent catalysis by flavin

Authors :: Grubber, Todd D.
Westler, William M.
Kiessling, Laura L.
Forest, Katrina T.
Source :: Biochemistry. Oct 6, 2009, Vol. 48 Issue 39, 9171-9173
Publication Year :: 2009
Abstract: The flavoenzyme uridine 5'-diphosphate galactopyranose mutase (UGM of Glf) has catalyzed the interconversion of UDP-galactopyranose and UDP-galactofuranose and the mechanistic studies of UGM have shown a novel role for the flavin. The X-ray crystal structures of the substrate-bound enzyme are described in oxidized and reduced forms, respectively.

Subjects :: Enzyme binding -- Analysis
Furanoses -- Chemical properties
Furanoses -- Structure
Pyranoses -- Structure
Pyranoses -- Chemical properties
Vitamin B2 -- Chemical properties
Uridine -- Chemical properties
X-ray crystallography -- Usage
Biological sciences
Chemistry

Tools