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Literature summary for 3.2.1.18 extracted from

  • Amaya, M.F.; Watts, A.G.; Damager, I.; Wehenkel, A.; Nguyen, T.; Buschiazzo, A.; Paris, G.; Frasch, A.C.; Withers, S.G.; Alzari, P.M.
    Structural insights into the catalytic mechanism of Trypanosoma cruzi trans-sialidase (2004), Structure, 12, 775-784.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
wild-type and mutant D59A, complexed with 2 mM 3-deoxy-N-acetylneuraminic acid to give a covalent intermediate, in 2 M ammonium sulfate, 100 mM HEPES, pH 8.0, 2%PEG 400, used for microseeding, in 10% PEG 4000, 100 mM Tris-HCl, pH 7.5, and 5% isopropanol, soaking in buffer with 5 mM 2,3-difluoro-sialic acid at 25°C, soaking in buffer containing 10 mM alpha-(2-3)-sialyllactose or 2'(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid, freezing and X-ray diffraction structure determination and analysis at 1.6 A Trypanosoma cruzi

Protein Variants

Protein Variants Comment Organism
D59A catalytic acid/base residue mutation, crystal structure determination, altered catalytic mechanism and enzyme-substrate structure compared to the wild-type enzyme, respectively Trypanosoma cruzi
additional information introduction of 7 surface mutations does not alter the enzymes' activities but facilitate crystallization Trypanosoma cruzi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information analysis of Michaelis enzyme-substrate complexes Trypanosoma cruzi

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
alpha(2-3)-sialyllactose + H2O Trypanosoma cruzi
-
sialic acid + lactose
-
?

Organism

Organism UniProt Comment Textmining
Trypanosoma cruzi
-
trans-sialidase
-

Reaction

Reaction Comment Organism Reaction ID
colominic acid + H2O = sialic acid + lactose trans-sialidase preferring the transfer of sialic acids from sialoglycoconjugates to beta-galactosyl acceptor molecules, ping-pong, double diplacement catalytic mechanism, Tyr342 is important, Asp59 is the acid/base residue, enzyme-substrate complex structure, covalent sialyl-enzyme intermediate Trypanosoma cruzi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid + H2O
-
Trypanosoma cruzi 4-methylumbelliferol + alpha-D-N-acetylneuraminic acid
-
?
alpha(2-3)-sialyllactose + H2O
-
Trypanosoma cruzi sialic acid + lactose
-
?
alpha(2-3)-sialyllactose + H2O formation of a covalent sialyl-enzyme intermediate Trypanosoma cruzi sialic acid + lactose
-
?
additional information the enzyme also performs transglycosylation reactions Trypanosoma cruzi ?
-
?

Synonyms

Synonyms Comment Organism
More enzyme belongs to the sialidase superfamily Trypanosoma cruzi
TcTS
-
Trypanosoma cruzi
trans-sialidase
-
Trypanosoma cruzi

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Trypanosoma cruzi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
assay at Trypanosoma cruzi