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Literature summary for 4.2.1.11 extracted from

  • Nakada, T.; Nagano, I.; Wu, Z.; Takahashi, Y.
    Molecular cloning and functional expression of enolase from Trichinella spiralis (2005), Parasitol. Res., 96, 354-360.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli strain DH5alpha with His-tag, recombinant enzyme without enolase activity, gaines activity after cutting off the signal peptide from the full-length protein Trichinella spiralis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
46000
-
recombinant enzyme, Western blotting Trichinella spiralis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-phospho-D-glycerate Trichinella spiralis
-
phosphoenolpyruvate + H2O
-
r
2-phospho-D-glycerate Trichinella spiralis ISS413
-
phosphoenolpyruvate + H2O
-
r

Organism

Organism UniProt Comment Textmining
Trichinella spiralis
-
-
-
Trichinella spiralis ISS413
-
-
-

Purification (Commentary)

Purification (Comment) Organism
muscle-stage larvae isolated by pepsin-HCl digestion from mice, recombinant enzyme by His Trap chelating column Trichinella spiralis

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Trichinella spiralis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-phospho-D-glycerate
-
Trichinella spiralis phosphoenolpyruvate + H2O
-
r
2-phospho-D-glycerate
-
Trichinella spiralis ISS413 phosphoenolpyruvate + H2O
-
r

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
-
Trichinella spiralis

pH Range

pH Minimum pH Maximum Comment Organism
6 7.5
-
Trichinella spiralis