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Results 1 - 7 of 7
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EC Number Inhibitors Commentary Structure
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.183CMP-N-acetylneuraminic acid - Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.183CMP-Neu5Ac feedback-inhibits the UDPGlcNAc 2-epimerase activity of GNE by binding to its allosteric site Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.183CMP-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 Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.183CMP-Neu5Ac feedback inhibition, cooperative binding mode and binding structure, overview Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.183CMP-sialic acid feedback inhibition Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.183UDP allosteric inhibition of enzyme GNE Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.183UDP 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 Go to the Ligand Summary Page
Results 1 - 7 of 7
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