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Literature summary extracted from

  • Seemann, J.E.; Schulz, G.E.
    Structure and mechanism of L-fucose isomerase from Escherichia coli (1997), J. Mol. Biol., 273, 256-268.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.1.3 overexpression in Escherichia coli Escherichia coli
5.3.1.25 overexpression in Escherichia coli Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.3.1.3 64976
-
 6 * 64976, crystallographic data Escherichia coli
5.3.1.3 390000
-
-
 Escherichia coli
5.3.1.25 64976
-
 6 * 64976, crystallographic data Escherichia coli
5.3.1.25 390000
-
-
 Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.3 Escherichia coli
-
-
-
5.3.1.25 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.1.3
-
 Escherichia coli
5.3.1.25
-
 Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
5.3.1.3 D-Arabinose = D-ribulose protein environment suggests strongly that the reaction belongs to the ene-diol type Escherichia coli
a
5.3.1.25 L-fucopyranose = L-fuculose protein environment suggests strongly that the reaction belongs to the ene-diol type Escherichia coli
a

Subunits

EC Number Subunits Comment Organism
5.3.1.3 hexamer 6 * 64976, crystallographic data Escherichia coli
5.3.1.25 hexamer 6 * 64976, crystallographic data Escherichia coli