Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Ko, T.P.; Lai, S.J.; Hsieh, T.J.; Yang, C.S.; Chen, Y.
    The tetrameric structure of sialic-acid-synthesizing UDP-GlcNAc 2-epimerase from Acinetobacter baumannii a comparative study with human GNE (2018), J. Biol. Chem., 293, 10119-10127 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.183 additional information the binding of UDP-GlcNAc to an allosteric site may stabilize the closed, active conformation of the enzyme, whereas the open form seems to be not active Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.183 D143A the GNE catalytic site mutant completely loses its activity Homo sapiens

General Stability

EC Number General Stability Organism
3.2.1.183 the binding of UDP-GlcNAc to an allosteric site may stabilize the closed, active conformation of the enzyme, whereas the open form seems to be not active Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
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 Homo sapiens
3.2.1.183 UDP allosteric inhibition of enzyme GNE Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.183 UDP-N-acetyl-alpha-D-glucosamine + H2O Homo sapiens
-
 N-acetyl-D-mannosamine + UDP
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.183 Homo sapiens Q9Y223
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.183 UDP-N-acetyl-alpha-D-glucosamine + H2O = N-acetyl-D-mannosamine + UDP catalytic and regulatory mechanisms Homo sapiens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.183 UDP-N-acetyl-alpha-D-glucosamine + H2O
-
 Homo sapiens N-acetyl-D-mannosamine + UDP
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.183 dimer
-
 Homo sapiens
3.2.1.183 More the epimerase part of the bifunctional UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE) folds into two Rossmann-like domains and forms dimers and tetramers Homo sapiens
3.2.1.183 tetramer
-
 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.2.1.183 bifunctional UDP-GlcNAc 2-epimerase/ManNAc kinase
-
 Homo sapiens
3.2.1.183 bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase UniProt Homo sapiens
3.2.1.183 GNE
-
 Homo sapiens
3.2.1.183 hydrolyzing epimerase
-
 Homo sapiens
3.2.1.183 hydrolyzing UDP-GlcNAc 2-epimerase
-
 Homo sapiens
3.2.1.183 More cf. EC 2.7.1.60 Homo sapiens
3.2.1.183 UDP-GlcNAc 2-epimerase
-
 Homo sapiens
3.2.1.183 UDP-GlcNAc-2-epimerase/ManAc kinase UniProt Homo sapiens

General Information

EC Number General Information Comment Organism
3.2.1.183 malfunction impaired feed-back inhibition of the enzyme by CMP-Neu5Ac to regulate the GNE activity can result in sialuria Homo sapiens
3.2.1.183 metabolism the biosynthesis of sialic acids starts with hydrolytic epimerization of N-acetyl glucosamine (GlcNAc), catalyzed by UDP-GlcNAc 2-epimerase and producing N-acetyl mannosamine (ManNAc), which then reacts with phosphoenolpyruvate to form Neu5Ac. Whereas the substrate for non-hydrolyzing epimerase and hydrolyzing epimerase is the same, in this case, UDP-GlcNAc, the product of the former is UDP-ManNAc, and that of the latter is alpha-ManNAc plus UDP Homo sapiens
3.2.1.183 additional information the binding of UDP-GlcNAc to an allosteric site may stabilize the closed, active conformation of the enzyme, whereas the open form seems to be not active. Residue D143 is essential for catalytic activity Homo sapiens