EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.2.1.18 | 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 |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.18 | 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 |
3.2.1.18 | additional information | introduction of 7 surface mutations does not alter the enzymes' activities but facilitate crystallization | Trypanosoma cruzi |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.18 | additional information | - |
additional information | analysis of Michaelis enzyme-substrate complexes | Trypanosoma cruzi |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.18 | alpha(2-3)-sialyllactose + H2O | Trypanosoma cruzi | - |
sialic acid + lactose | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.18 | Trypanosoma cruzi | - |
trans-sialidase | - |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.2.1.18 | 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 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.18 | 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid + H2O | - |
Trypanosoma cruzi | 4-methylumbelliferol + alpha-D-N-acetylneuraminic acid | - |
? | |
3.2.1.18 | alpha(2-3)-sialyllactose + H2O | - |
Trypanosoma cruzi | sialic acid + lactose | - |
? | |
3.2.1.18 | alpha(2-3)-sialyllactose + H2O | formation of a covalent sialyl-enzyme intermediate | Trypanosoma cruzi | sialic acid + lactose | - |
? | |
3.2.1.18 | additional information | the enzyme also performs transglycosylation reactions | Trypanosoma cruzi | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.18 | More | enzyme belongs to the sialidase superfamily | Trypanosoma cruzi |
3.2.1.18 | TcTS | - |
Trypanosoma cruzi |
3.2.1.18 | trans-sialidase | - |
Trypanosoma cruzi |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.18 | 25 | - |
assay at | Trypanosoma cruzi |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.18 | 7.2 | - |
assay at | Trypanosoma cruzi |