EC Number |
Inhibitors |
Structure |
---|
3.2.1.183 | CMP-N-acetylneuraminic acid |
- |
|
3.2.1.183 | CMP-Neu5Ac |
feedback-inhibits the UDPGlcNAc 2-epimerase activity of GNE by binding to its allosteric site |
|
3.2.1.183 | CMP-Neu5Ac |
the downstream product CMP-Neu5Ac also acts as a feed-back inhibitor to regulate the GNE activity. The feedback inhibitor binds to the dimer-dimer interface and locks the tetramer into a tightly closed and inactive conformation. This is distinct from the activation mechanism of the non-hydrolyzing enzyme through a closed conformation |
|
3.2.1.183 | CMP-Neu5Ac |
feedback inhibition, cooperative binding mode and binding structure, overview |
|
3.2.1.183 | CMP-sialic acid |
feedback inhibition |
|
3.2.1.183 | UDP |
allosteric inhibition of enzyme GNE |
|
3.2.1.183 | UDP |
the binding mode of UDP reveals unique interactions with the hydrolyzing epimerase, binding structure, overview. The base is sandwiched between the side chains of Arg19 and Phe287, while making two hydrogen bonds to the backbone of Val282. The two hydroxyl groups of ribose are hydrogen bonded to the side chains of Ser23 and Glu307. The diphosphate forms salt bridges to Arg19, Arg113 and Arg321. It also interacts with His220 and Asn253 through hydrogen bonds, as well as the two consecutive Ser301 and Ser302 at the N-terminus of helix alpha12 |
|