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Information on EC 4.2.1.115 - UDP-N-acetylglucosamine 4,6-dehydratase (configuration-inverting)

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IUBMB Comments
Contains NADP+ as a cofactor. This is 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. This enzyme plays a critical role in H. pylori's pathogenesis, being involved in the synthesis of both functional flagella and lipopolysaccharides [1,2]. It is 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. This enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes.
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The enzyme appears in viruses and cellular organisms
Synonyms
4,6-dehydratase/5-epimerase, CapE, Cj1293, FlaA1, HP0840, inverting 4,6-dehydratase, Mg534, More, NAD(P)+-dependent dehydratase/epimerase, PseB, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine = UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
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