Literature summary for 3.2.1.18 extracted from

Harrison, J.A.; Kartha, K.P.; Fournier, E.J.; Lowary, T.L.; Malet, C.; Nilsson, U.J.; Hindsgaul, O.; Schenkman, S.; Naismith, J.H.; Field, R.A.
Probing the acceptor substrate binding site of Trypanosoma cruzi trans-sialidase with systematically modified substrates and glycoside libraries (2011), Org. Biomol. Chem., 9, 1653-1660.

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Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	construction of octyl galactosides and octyl N-acetyl-lactosamines as trans-sialidase inhibitors, inhibitor screening of the beta-thiogalactopyranoside library, overview	Trypanosoma cruzi

Organism

Organism	UniProt	Comment	Textmining
Trypanosoma cruzi	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme catalyses the alpha-(2,3)-sialylation of non-reducing terminal beta-galactose residues, it is largely intolerant of substitution of the galactose 2 and 4 positions whereas substitution of the galactose 6 position is well tolerated, even the addition of a bulky sugar residue, glucose or galactose, does not impact negatively on TcTS binding and turnover, which highlights the potential of internal 6-substituted galactose residues to serve as enzyme acceptor substrates, substrate binding mode and site, overview	Trypanosoma cruzi	?	-	?

Synonyms

Synonyms	Comment	Organism
trans-sialidase	-	Trypanosoma cruzi

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Trypanosoma cruzi

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Trypanosoma cruzi

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Release 2023.1 (January 2023)