Literature summary for 3.2.1.18 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.

Search for more literature for 3.2.1.18

Activating Compound

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

Cloned(Commentary)

Cloned (Comment)	Organism
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]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
3.1	-	4-methylumbelliferyl D-N-acetylneuraminyl-alpha-(2->3)-D-galactopyranoside	pH 3.5, 37°C	Aspergillus fumigatus
3.3	-	4-methylumbelliferyl alpha-D-N-acetylneuraminic acid	pH 3.5, 37°C	Aspergillus fumigatus

Localization

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism	UniProt	Comment	Textmining
Aspergillus fumigatus	-	-	-
Aspergillus fumigatus Af293	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	the enzyme contains potential N-glycosylation sites, e.g. a one low scoring Nglycosylation site at Asn 215	Aspergillus fumigatus

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme from Escherichia coli strain Tuner (DE3) by nickel affinity chromatography and gel filtration	Aspergillus fumigatus

Source Tissue

Source Tissue	Comment	Organism	Textmining
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]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.00012	-	purified recombinant enzyme, substrate 4-methylumbelliferyl D-N-acetylneuraminyl-alpha-(2->3)-D-galactopyranoside, pH 3.5, 37°C	Aspergillus fumigatus
0.0409	-	purified recombinant enzyme, substrate 4-methylumbelliferyl alpha-D-N-acetylneuraminic acid, pH 3.5, 37°C	Aspergillus fumigatus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4-methylumbelliferyl alpha-D-N-acetylneuraminic acid + H2O	-	Aspergillus fumigatus	4-methylumbelliferol + alpha-D-N-acetylneuraminic acid	-	?
4-methylumbelliferyl alpha-D-N-acetylneuraminic acid + H2O	-	Aspergillus fumigatus Af293	4-methylumbelliferol + alpha-D-N-acetylneuraminic acid	-	?
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	-	?
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	-	?
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	?	-	?
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

Subunits	Comment	Organism
?	x * 42000, SDS-PAGE	Aspergillus fumigatus
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]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.0004	-	4-methylumbelliferyl D-N-acetylneuraminyl-alpha-(2->3)-D-galactopyranoside	pH 3.5, 37°C	Aspergillus fumigatus
0.0743	-	4-methylumbelliferyl alpha-D-N-acetylneuraminic acid	pH 3.5, 37°C	Aspergillus fumigatus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
3.5	-	-	Aspergillus fumigatus

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
144	-	4-methylumbelliferyl D-N-acetylneuraminyl-alpha-(2->3)-D-galactopyranoside	pH 3.5, 37°C	Aspergillus fumigatus
22300	-	4-methylumbelliferyl alpha-D-N-acetylneuraminic acid	pH 3.5, 37°C	Aspergillus fumigatus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)