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Literature summary extracted from

  • Manjasetty, B.A.; Chance, M.R.
    Crystal structure of Escherichia coli L-arabinose isomerase (ECAI), the putative target of biological tagatose production (2006), J. Mol. Biol., 360, 297-309.
    View publication on PubMed

Application

EC Number Application Comment Organism
5.3.1.4 food industry production of D-tagatose as a low-calorie sugar-substituting sweetener Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.1.4 expression in Escherichia coli of the selenomethionine-substituted enzyme Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.3.1.4 of the enzyme in its apoform Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.3.1.4 56040
-
-
 Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.4 Escherichia coli P08202
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.1.4 of the recombinant enzyme by Ni-NTA-agarose resin chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.1.4 D-galactose
-
 Escherichia coli D-tagatose
-
 ?
5.3.1.4 L-arabinose
-
 Escherichia coli L-ribulose
-
 ?

Subunits

EC Number Subunits Comment Organism
5.3.1.4 hexamer as revealed by the three domain crystal structure Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
5.3.1.4 D-galactose isomerase
-
 Escherichia coli
5.3.1.4 ECAI Escherichia coli L-arabinose isomerase Escherichia coli
5.3.1.4 L-arabinose aldose-ketose-isomerase
-
 Escherichia coli
5.3.1.4 L-arabinose isomerase
-
 Escherichia coli