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ENZYME entry: EC 4.2.1.115

Accepted Name
UDP-N-acetylglucosamine 4,6-dehydratase (inverting).
Alternative Name(s)
UDP-N-acetylglucosamine 5-inverting 4,6-dehydratase.
Reaction catalysed
UDP-N-acetyl-alpha-D-glucosamine <=> UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H(2)O
Cofactor(s)
NADPH.
Comment(s)
  • 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.
Cross-references
BRENDA4.2.1.115
EC2PDB4.2.1.115
ExplorEnz4.2.1.115
PRIAM enzyme-specific profiles4.2.1.115
KEGG Ligand Database for Enzyme Nomenclature4.2.1.115
IUBMB Enzyme Nomenclature4.2.1.115
IntEnz4.2.1.115
MEDLINEFind literature relating to 4.2.1.115
MetaCyc4.2.1.115
UniProtKB/Swiss-Prot
Q0P8W4, PSEB_CAMJE;  Q5QKR8, PSEB_CAMJJ;  O25511, PSEB_HELPY;  

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All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.2.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.2.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.-.-.-