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Literature summary extracted from

  • Morley, T.J.; Willis, L.M.; Whitfield, C.; Wakarchuk, W.W.; Withers, S.G.
    A new sialidase mechanism: bacteriophage K1F endo-sialidase is an inverting glycosidase (2009), J. Biol. Chem., 284, 17404-17410.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.18 expressed in Escherichia coli Escherichia phage K1F
3.2.1.129 expressed in Escherichia coli BL21(DE3) cells Escherichia phage K1F

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.18 E581A the mutation results in complete loss of sialidase activity Escherichia phage K1F
3.2.1.129 E581A the mutation results in complete loss of sialidase activity Escherichia phage K1F

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.129 0.68
-
 trifluoromethylumbelliferyl sialotrioside at pH 4.5 Escherichia phage K1F

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.18 additional information Escherichia phage K1F endoNF is therefore an inverting glycosidase ?
-
 ?
3.2.1.18 polysialic acid + H2O Escherichia phage K1F
-
 sialic acid
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.18 Escherichia phage K1F
-
-
-
3.2.1.129 Escherichia phage K1F
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.18 amylose resin column chromatography Escherichia phage K1F
3.2.1.129 amylose resin column chromatography, gel filtration Escherichia phage K1F

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.18 alpha(2-6)-sialyllactose + H2O
-
 Escherichia phage K1F sialic acid + lactose
-
 ?
3.2.1.18 additional information endoNF is therefore an inverting glycosidase Escherichia phage K1F ?
-
 ?
3.2.1.18 additional information does not hydrolyze the monomeric and dimeric sialic acid with alpha-linked trifluoromethylumbelliferyl significantly over a 2 h period Escherichia phage K1F ?
-
 ?
3.2.1.18 polysialic acid + H2O
-
 Escherichia phage K1F sialic acid
-
 ?
3.2.1.18 sialic acid tetramer with alpha-linked trifluoromethylumbelliferyl + H2O hydrolysis with formation of two alpha-linked trifluoromethylumbelliferyl glycoside-containing species, trifluoromethylumbelliferone and the TFMU sialoside monomer Escherichia phage K1F ?
-
 ?
3.2.1.18 sialic acid trimer with alpha-linked trifluoromethylumbelliferyl + H2O degraded with exclusive cleavage at the coumarin-sialoside bond Escherichia phage K1F ?
-
 ?
3.2.1.129 additional information the endo-sialidase requires the occupation of a minimum of three subsites by sialic acid for efficient catalysis, so neither monomer (trifluoromethylumbelliferyl sialoside) nor dimer (trifluoromethylumbelliferyl sialobioside) are hydrolyzed by endoNF Escherichia phage K1F ?
-
 ?
3.2.1.129 poly(sialic) acid + H2O
-
 Escherichia phage K1F fragments of poly(sialic) acid
-
 ?
3.2.1.129 trifluoromethylumbelliferyl sialotetraoside + H2O
-
 Escherichia phage K1F trifluoromethylumbelliferone + sialotetraoside
-
 ?
3.2.1.129 trifluoromethylumbelliferyl sialotrioside + H2O
-
 Escherichia phage K1F trifluoromethylumbelliferone + sialotrioside
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.18 endo-sialidase
-
 Escherichia phage K1F
3.2.1.18 endoNF
-
 Escherichia phage K1F
3.2.1.129 endo-sialidase
-
 Escherichia phage K1F
3.2.1.129 endoNF endoNF is an inverting sialidase Escherichia phage K1F

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.129 1.28
-
 trifluoromethylumbelliferyl sialotrioside at pH 4.5 Escherichia phage K1F

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.129 4.5
-
-
 Escherichia phage K1F