CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.25 | UDP-galactose 4-epimerase; domain 1 |
|
3.90.25.30 | Polysaccharide biosynthesis protein, CapD-like domain |
Domain Context
CATH Clusters
| Superfamily | Polysaccharide biosynthesis protein, CapD-like domain |
| Functional Family |
Enzyme Information
| 4.2.1.115 |
UDP-N-acetylglucosamine 4,6-dehydratase (inverting).
based on mapping to UniProt O25511
UDP-N-acetyl-alpha-D-glucosamine = UDP-2-acetamido-2,6-dideoxy-beta-L- arabino-hex-4-ulose + H(2)O.
-!- The first enzyme in the biosynthetic pathway of pseudaminic acid, a sialic-acid-like sugar that is unique to bacteria and is used by Helicobacter pylori to modify its flagellin. -!- Plays a critical role in H.pylori's pathogenesis, being involved in the synthesis of both functional flagella and lipopolysaccharides. -!- Completely inhibited by UDP-alpha-D-galactose. -!- The reaction results in the chirality of the C-5 atom being inverted. -!- It is thought that Lys-133 acts sequentially as a catalytic acid, protonating the C-6 hydroxy group and as a catalytic base, abstracting the C-5 proton, resulting in the elimination of water.
|
UniProtKB Entries (1)
| O25511 |
PSEB_HELPY
Helicobacter pylori 26695
UDP-N-acetylglucosamine 4,6-dehydratase (inverting)
|
PDB Structure
| PDB | 2GN8 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural Studies of FlaA1 from Helicobacter pylori Reveal the Mechanism for Inverting 4,6-Dehydratase Activity.
J.Biol.Chem.
|
