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Literature summary extracted from

  • Warwas, M.L.; Yeung, J.H.; Indurugalla, D.; Mooers, A.O.; Bennet, A.J.; Moore, M.M.
    Cloning and characterization of a sialidase from the filamentous fungus, Aspergillus fumigatus (2010), Glycoconj. J., 27, 533-548.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.18 additional information bovine serum albumin does not increase enzyme activity Aspergillus fumigatus

Cloned(Commentary)

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

KM Value [mM]

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

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.18 extracellular the enzyme contains a 20 amino acid signal peptide Aspergillus fumigatus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.18 additional information CaCl2, MgCl2 or MnCl2 do not increase enzyme activity Aspergillus fumigatus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.18 42000
-
 x * 42000, SDS-PAGE Aspergillus fumigatus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.18 Aspergillus fumigatus
-
-
-
3.2.1.18 Aspergillus fumigatus Af293
-
-
-

Posttranslational Modification

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

Purification (Commentary)

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

Source Tissue

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
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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 ?
-
 ?

Subunits

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.18 37
-
 assay at Aspergillus fumigatus

Turnover Number [1/s]

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.18 3.5
-
-
 Aspergillus fumigatus

kcat/KM [mM/s]

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