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Literature summary extracted from

  • Ferreira, L.; Munoz-Barroso, I.; Marcos, F.; Shnyrov, V.L.; Villar, E.
    Sialidase, receptor-binding and fusion-promotion activities of Newcastle disease virus haemagglutinin-neuraminidase glycoprotein: a mutational and kinetic study (2004), J. Gen. Virol., 85, 1981-1988.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.18 transient expression of wild-type and mutant enzymes in HeLa cells, cell surface orientation Avian orthoavulavirus 1

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.18 E258D site-directed mutagenesis, mutation of a catalytic residue, highly reduced sialidase activity, slightly reduced HA activity, mutant shows reduced fusion promotion activity Avian orthoavulavirus 1
3.2.1.18 R498K site-directed mutagenesis, mutation of a catalytic residue, reduced sialidase activity, slightly reduced HA activity, mutant shows reduced fusion promotion activity Avian orthoavulavirus 1
3.2.1.18 R498Q site-directed mutagenesis, mutation of a catalytic residue, highly reduced sialidase activity, slightly reduced HA activity, mutant shows reduced fusion promotion activity Avian orthoavulavirus 1
3.2.1.18 S418A site-directed mutagenesis, mutation of a catalytic residue, unaltered sialidase activity, altered HA activity, mutant shows reduced fusion promotion activity Avian orthoavulavirus 1
3.2.1.18 Y262F site-directed mutagenesis, mutation of a catalytic residue, retaining of nearly all sialidase activity, altered HA activity, mutant shows reduced fusion promotion activity Avian orthoavulavirus 1
3.2.1.18 Y262S site-directed mutagenesis, mutation of a catalytic residue, loss of nearly all sialidase activity, highly reduced HA activity, mutant shows reduced fusion promotion activity Avian orthoavulavirus 1
3.2.1.18 Y317A site-directed mutagenesis, mutation of a catalytic residue, loss of nearly all sialidase activity, highly reduced HA activity, mutant shows reduced fusion promotion activity Avian orthoavulavirus 1
3.2.1.18 Y317F site-directed mutagenesis, mutation of a catalytic residue, reduced sialidase activity, altered HA activity, mutant shows reduced fusion promotion activity Avian orthoavulavirus 1
3.2.1.18 Y317S site-directed mutagenesis, mutation of a catalytic residue, highly reduced sialidase activity, highly reduced HA activity, mutant shows reduced fusion promotion activity Avian orthoavulavirus 1

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.18 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid substrate inhibition Avian orthoavulavirus 1

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.18 additional information
-
 additional information kinetics and thermodynamics of wild-type and mutant enzymes Avian orthoavulavirus 1
3.2.1.18 0.5
-
 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid pH 7.5, wild-type enzyme Avian orthoavulavirus 1
3.2.1.18 1.1
-
 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid pH 7.5, mutant S418A Avian orthoavulavirus 1
3.2.1.18 4.9
-
 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid pH 7.5, mutant Y262F Avian orthoavulavirus 1

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.18 plasma membrane
-
 Avian orthoavulavirus 1 5886
-

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.18 Avian orthoavulavirus 1 Q9Q2W5 Clone 30 strain
-
3.2.1.18 Avian orthoavulavirus 1 Kansas Q9Q2W5 Clone 30 strain
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.18 colominic acid + H2O = sialic acid + lactose active site, Arg498, Glu258, Tyr317, and Tyr262 are catalytic residues, with the aromatic ring of the latter being important for function Avian orthoavulavirus 1
a

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 additional information
-
 activities of diverse mutants, overview Avian orthoavulavirus 1

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
-
 Avian orthoavulavirus 1 4-methylumbelliferol + alpha-D-N-acetylneuraminic acid
-
 ?
3.2.1.18 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid + H2O
-
 Avian orthoavulavirus 1 Kansas 4-methylumbelliferol + alpha-D-N-acetylneuraminic acid
-
 ?
3.2.1.18 additional information multifunctional enzyme with sialidase, receptor-binding, and fusion promotion activities Avian orthoavulavirus 1 ?
-
 ?
3.2.1.18 additional information multifunctional enzyme with sialidase, receptor-binding, and fusion promotion activities Avian orthoavulavirus 1 Kansas ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.18 haemagglutinin-neuraminidase protein
-
 Avian orthoavulavirus 1
3.2.1.18 HN
-
 Avian orthoavulavirus 1

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.18 7.5
-
 assay at Avian orthoavulavirus 1

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.1.18 16.2
-
 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid pH 7.5, mutant S418A Avian orthoavulavirus 1
3.2.1.18 24.7
-
 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid pH 7.5, wild-type enzyme Avian orthoavulavirus 1
3.2.1.18 28.1
-
 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid pH 7.5, mutant Y262F Avian orthoavulavirus 1