Literature summary for 5.1.3.14 extracted from

Blume, A.; Chen, H.; Reutter, W.; Schmidt, R.R.; Hinderlich, S.
2',3'-Dialdehydo-UDP-N-acetylglucosamine inhibits UDP-N-acetylglucosamine 2-epimerase, the key enzyme of sialic acid biosynthesis (2002), FEBS Lett., 521, 127-132.

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Inhibitors

Inhibitors	Comment	Organism	Structure
2',3'-dialdehydro-ADP	efficient inhibition is most likely due to the structural similarity to o-UDP and not to an allosteric effect via the ATP binding site	Rattus norvegicus
2',3'-dialdehydro-UDP	binds to the active site of the enzyme	Rattus norvegicus
2',3'-dialdehydro-UDP-alpha-D-N-acetylglucosamine	0.05 mM, 70% inhibition after 30 min. 0.25 mM, 90% inhibition. Covalently bound to amino acids in the active site causing an irreversible inhibition. Effective inhibitor may serve as a basis for the chemical synthesis of further inhibitors	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	enzyme catalyzes the first step in synthesis of sialic acids	Rattus norvegicus	?	-	?

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Release 2023.1 (January 2023)