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Literature summary for 5.3.1.4 extracted from

  • Wallace, L.J.; Eiserling, F.A.; Wilcox, G.
    The shape of L-arabinose isomerase from Escherichia coli (1978), J. Biol. Chem., 253, 3717-3720.
    View publication on PubMed
Search for more literature for 5.3.1.4

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60000
-
 6 * 60000, sedimentation in the ultracentrifuge in presence of 8 M urea or pH 2 phosphate buffer Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-Arabinose Escherichia coli catalyzes the first step in catabolism of L-arabinose ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 temperature-sensitive mutant
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arabinose
-
 Escherichia coli L-ribulose
-
 ?
L-Arabinose catalyzes the first step in catabolism of L-arabinose Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
hexamer the enzyme is seen in two distinctly different orientations: the first has three subunits visible, with a 3fold axis of symmetry, corresponding to a face-on view of two stacked, eclipsed trimers. The second orientation is rectangular in shape with 2fold symmetry, suggesting a side-one view of the stacked trimers Escherichia coli
hexamer 6 * 60000, sedimentation in the ultracentrifuge in presence of 8 M urea or pH 2 phosphate buffer Escherichia coli