Literature summary for 3.2.1.18 extracted from

Terada, T.; Kitajima, K.; Inoue, S.; Wilson, J.C.; Norton, A.K.; Kong, D.C.M.; Thomson, R.J.; von Itzstein, M.; Inoue, Y.
Catalysis by a new sialidase, deaminoneuraminic acid residue-cleaving enzyme (KDNase Sm), initially forms a less stable alpha-anomer of 3-deoxy-D-glycero-D-galacto-nonulosonic acid and is strongly inhibited by the transition state analogue, 2-deoxy-2,3-didehydro-D-glycero-D-galacto-2-nonulopyranosonic acid, but not by 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (1997), J. Biol. Chem., 272, 5452-5456.

Inhibitors

Inhibitors	Comment	Organism	Structure
2-deoxy-2,3-didehydro-D-glycero-D-galacto-2-nonulopyranosonic acid	-	Sphingobacterium multivorum

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.04	-	4-methylumbelliferyl-3-deoxy-D-glycero-D-galactononulosonic acid	-	Sphingobacterium multivorum

Organism	UniProt	Comment	Textmining
Sphingobacterium multivorum	-	-	-

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4-methylumbelliferyl-3-deoxy-D-glycero-D-galacto-2-nonulosonic acid + H2O	-	Sphingobacterium multivorum	?	-	?
4-methylumbelliferyl-3-deoxy-D-glycero-D-galactononulosonic acid + H2O	-	Sphingobacterium multivorum	4-methylumbelliferone + 3-deoxy-D-glycero-D-galactononulosonic acid	-	?

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Release 2023.1 (January 2023)