Expasy logo

ENZYME

ENZYME entry: EC 4.2.1.115

PURL: https://purl.expasy.org/enzyme/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 + H2O
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
KEGG Ligand Database for Enzyme Nomenclature4.2.1.115
IUBMB Enzyme Nomenclature4.2.1.115
MEDLINEFind literature relating to 4.2.1.115
MetaCyc4.2.1.115
Rhea expert-curated reactions4.2.1.115
UniProtKB/Swiss-Prot
Q0P8W4, PSEB_CAMJEQ5QKR8, PSEB_CAMJJO25511, PSEB_HELPY

View entry in original ENZYME format
View entry in raw text format (no links)
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.-.-.-