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Literature summary extracted from

  • Rhimi, M.; Juy, M.; Aghajari, N.; Haser, R.; Bejar, S.
    Probing the essential catalytic residues and substrate affinity in the thermoactive Bacillus stearothermophilus US100 L-arabinose isomerase by site-directed mutagenesis (2007), J. Bacteriol., 189, 3556-3563.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
5.3.1.4 food industry production of D-tagatose Geobacillus stearothermophilus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.1.4 expression in Escherichia coli Geobacillus stearothermophilus

Protein Variants

EC Number Protein Variants Comment Organism
5.3.1.4 D308A site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 E306A site directed mutagenesis, no activity Geobacillus stearothermophilus
5.3.1.4 E331A site directed mutagenesis, no activity Geobacillus stearothermophilus
5.3.1.4 E351A site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 F279Q site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 F329A site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 H348A site directed mutagenesis, no activity Geobacillus stearothermophilus
5.3.1.4 H446A site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 H447A site directed mutagenesis, no activity Geobacillus stearothermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.3.1.4 28.42
-
 L-arabinose wild type Geobacillus stearothermophilus
5.3.1.4 29.3
-
 L-arabinose D308A mutant Geobacillus stearothermophilus
5.3.1.4 30.1
-
 L-arabinose E351A mutant Geobacillus stearothermophilus
5.3.1.4 30.4
-
 L-arabinose H446A mutant Geobacillus stearothermophilus
5.3.1.4 30.6
-
 L-arabinose F329A mutant Geobacillus stearothermophilus
5.3.1.4 79.7
-
 L-arabinose F279Q mutant Geobacillus stearothermophilus
5.3.1.4 173.6
-
 L-fucose F279Q mutant Geobacillus stearothermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.3.1.4 Mn2+ is closely bound to the protein even after treatment with EDTA Geobacillus stearothermophilus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.3.1.4 56000
-
 SDS-PAGE Geobacillus stearothermophilus

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.4 Geobacillus stearothermophilus Q9S467
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.1.4 of the recombinant mutant proteins Geobacillus stearothermophilus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.3.1.4 18
-
 fucose as substrate, F279Q mutant Geobacillus stearothermophilus
5.3.1.4 21
-
 D308A mutant Geobacillus stearothermophilus
5.3.1.4 27
-
 E351A mutant Geobacillus stearothermophilus
5.3.1.4 53
-
 F329A mutant Geobacillus stearothermophilus
5.3.1.4 79
-
 H446A mutant Geobacillus stearothermophilus
5.3.1.4 184
-
 wild type Geobacillus stearothermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.1.4 D-galactose
-
 Geobacillus stearothermophilus D-tagatose
-
 ?
5.3.1.4 L-arabinose
-
 Geobacillus stearothermophilus L-ribulose
-
 ?
5.3.1.4 L-Fucose only F279 mutant Geobacillus stearothermophilus L-Fuculose
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.3.1.4 D-galactose isomerase
-
 Geobacillus stearothermophilus
5.3.1.4 L-AI US100
-
 Geobacillus stearothermophilus
5.3.1.4 L-arabinose aldose-ketose-isomerase
-
 Geobacillus stearothermophilus
5.3.1.4 L-arabinose isomerase
-
 Geobacillus stearothermophilus