EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.18 | additional information | bovine serum albumin does not increase enzyme activity | Aspergillus fumigatus |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.18 | DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Tuner (DE3) | Aspergillus fumigatus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.18 | 3.1 | - |
4-methylumbelliferyl D-N-acetylneuraminyl-alpha-(2->3)-D-galactopyranoside | pH 3.5, 37°C | Aspergillus fumigatus | |
3.2.1.18 | 3.3 | - |
4-methylumbelliferyl alpha-D-N-acetylneuraminic acid | pH 3.5, 37°C | Aspergillus fumigatus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.2.1.18 | extracellular | the enzyme contains a 20 amino acid signal peptide | Aspergillus fumigatus | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.18 | additional information | CaCl2, MgCl2 or MnCl2 do not increase enzyme activity | Aspergillus fumigatus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.2.1.18 | 42000 | - |
x * 42000, SDS-PAGE | Aspergillus fumigatus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.18 | Aspergillus fumigatus | - |
- |
- |
3.2.1.18 | Aspergillus fumigatus Af293 | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.2.1.18 | glycoprotein | the enzyme contains potential N-glycosylation sites, e.g. a one low scoring Nglycosylation site at Asn 215 | Aspergillus fumigatus |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.1.18 | recombinant His-tagged enzyme from Escherichia coli strain Tuner (DE3) by nickel affinity chromatography and gel filtration | Aspergillus fumigatus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.2.1.18 | mycelium | the organism is unable to use either sialic acid or colominic acid as a sole source of carbon | Aspergillus fumigatus | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.2.1.18 | 0.00012 | - |
purified recombinant enzyme, substrate 4-methylumbelliferyl D-N-acetylneuraminyl-alpha-(2->3)-D-galactopyranoside, pH 3.5, 37°C | Aspergillus fumigatus |
3.2.1.18 | 0.0409 | - |
purified recombinant enzyme, substrate 4-methylumbelliferyl alpha-D-N-acetylneuraminic acid, pH 3.5, 37°C | Aspergillus fumigatus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.18 | 4-methylumbelliferyl alpha-D-N-acetylneuraminic acid + H2O | - |
Aspergillus fumigatus | 4-methylumbelliferol + alpha-D-N-acetylneuraminic acid | - |
? | |
3.2.1.18 | 4-methylumbelliferyl alpha-D-N-acetylneuraminic acid + H2O | - |
Aspergillus fumigatus Af293 | 4-methylumbelliferol + alpha-D-N-acetylneuraminic acid | - |
? | |
3.2.1.18 | 4-methylumbelliferyl D-N-acetylneuraminyl-alpha-(2->3)-D-galactopyranoside + H2O | preference for the alpha2-3 isomer of 4-methylumbelliferyl alpha-D-N-acetylneuraminylgalactopyranoside | Aspergillus fumigatus | 4-methylumbelliferol + N-acetylneuraminate + 4-methylumbelliferyl alpha-D-galactopyranoside | - |
? | |
3.2.1.18 | 4-methylumbelliferyl D-N-acetylneuraminyl-alpha-(2->3)-D-galactopyranoside + H2O | preference for the alpha2-3 isomer of 4-methylumbelliferyl alpha-D-N-acetylneuraminylgalactopyranoside | Aspergillus fumigatus Af293 | 4-methylumbelliferol + N-acetylneuraminate + 4-methylumbelliferyl alpha-D-galactopyranoside | - |
? | |
3.2.1.18 | additional information | the sialidase prefers alpha2-3-linked sialic acids over the alpha2-6 isomers. The enzyme shows no trans-sialidase activity. The purified sialidase releases sialic acid from diverse substrates such as mucin, fetuin, epithelial cell glycans and colominic acid, no activity with asialofetuin | Aspergillus fumigatus | ? | - |
? | |
3.2.1.18 | additional information | the sialidase prefers alpha2-3-linked sialic acids over the alpha2-6 isomers. The enzyme shows no trans-sialidase activity. The purified sialidase releases sialic acid from diverse substrates such as mucin, fetuin, epithelial cell glycans and colominic acid, no activity with asialofetuin | Aspergillus fumigatus Af293 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.2.1.18 | ? | x * 42000, SDS-PAGE | Aspergillus fumigatus |
3.2.1.18 | More | construction of a three dimensional model based on structural alignments and structural superposition on the sialidase from Micromonospora viridifaciens, PDB ID 1eus | Aspergillus fumigatus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.18 | 37 | - |
assay at | Aspergillus fumigatus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.18 | 0.0004 | - |
4-methylumbelliferyl D-N-acetylneuraminyl-alpha-(2->3)-D-galactopyranoside | pH 3.5, 37°C | Aspergillus fumigatus | |
3.2.1.18 | 0.0743 | - |
4-methylumbelliferyl alpha-D-N-acetylneuraminic acid | pH 3.5, 37°C | Aspergillus fumigatus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.18 | 3.5 | - |
- |
Aspergillus fumigatus |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.18 | 144 | - |
4-methylumbelliferyl D-N-acetylneuraminyl-alpha-(2->3)-D-galactopyranoside | pH 3.5, 37°C | Aspergillus fumigatus | |
3.2.1.18 | 22300 | - |
4-methylumbelliferyl alpha-D-N-acetylneuraminic acid | pH 3.5, 37°C | Aspergillus fumigatus |