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Literature summary for 4.2.1.11 extracted from

  • Esgleas, M.; Li, Y.; Hancock, M.A.; Harel, J.; Dubreuil, J.D.; Gottschalk, M.
    Isolation and characterization of alpha-enolase, a novel fibronectin-binding protein from Streptococcus suis (2008), Microbiology, 154, 2668-2679.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
subcloned in Escherichia coli Streptococcus suis

Localization

Localization Comment Organism GeneOntology No. Textmining
cell wall
-
Streptococcus suis 5618
-
cytoplasm
-
Streptococcus suis 5737
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52000
-
-
Streptococcus suis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-phospho-D-glycerate Streptococcus suis analysis of pathogenesis of Streptococcus suis: rSsEno binds to fibronectin and plasminogen phosphoenolpyruvate + H2O
-
r

Organism

Organism UniProt Comment Textmining
Streptococcus suis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Streptococcus suis

Source Tissue

Source Tissue Comment Organism Textmining
culture supernatant
-
Streptococcus suis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-phospho-D-glycerate analysis of pathogenesis of Streptococcus suis: rSsEno binds to fibronectin and plasminogen Streptococcus suis phosphoenolpyruvate + H2O
-
r

Synonyms

Synonyms Comment Organism
alpha-enolase
-
Streptococcus suis
rSsEno recombinant Streptococcus suis-enolase-protein with a His tag expressed in Escherichia coli Streptococcus suis
SsEno
-
Streptococcus suis