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Literature summary extracted from

  • Oh, D.K.; Oh, H.J.; Kim, H.J.; Cheon, J.; Kim, P.
    Modification of optimal pH in L-arabinose isomerase from Geobacillus stearothermophilus for D-galactose isomerization (2006), J. Mol. Catal. B, 43, 108-112.
No PubMed abstract available

Application

EC Number Application Comment Organism
5.3.1.4 food industry production of D-tagatose as a low-calorie sugar-substituting sweetener lower pH is preferable for industrial production 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 A408V site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 A408V/K475N site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 A475N site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 D228N site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 D228N/D384G/T393S/N428K/K475N site directed mutagenesis, GSAI 152 Geobacillus stearothermophilus
5.3.1.4 D384G site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 G408V site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 K475N site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 L408V site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 N428K site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 Q408V site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 Q475N site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 R408V site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 R475N site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 T393S site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 V322M site directed mutagenesis Geobacillus stearothermophilus
5.3.1.4 V322M/T393S/A408V site directed mutagenesis, GSAI 153 Geobacillus stearothermophilus

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.1.4 of the recombinant wild type and mutant enzymes 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 0.004
-
 D228N mutant, D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.029
-
 R408V mutant, D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.043
-
 wild type, D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.05
-
 L408V mutant, D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.056
-
 D384G mutant, D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.06
-
 Q408V mutant, at pH 7.5, D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.06
-
 R408V mutant, at pH 7.5, D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.062
-
 Q408V mutant, D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.11
-
 T393S mutant, D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.26
-
 N428K mutant, D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.27
-
 V322M mutant, D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.37
-
 G408V mutant, D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.37
-
 Q475N mutant, D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.38
-
 R475N mutant, D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.39
-
 K475N mutant found in GSAI152, D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.39
-
 K475N mutant, D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.48
-
 A408V mutant, D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.48
-
 A475N mutant found in GSAI153, D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.49
-
 GSAI1 152, D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.59
-
 A408V/K475N mutant found in GSAI152 or GASI 153w D-galactose as substrate Geobacillus stearothermophilus
5.3.1.4 0.74
-
 GSAI1 153, D-galactose as substrate 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
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.3.1.4 D-galactose isomerase
-
 Geobacillus stearothermophilus
5.3.1.4 GSAI Geobacillus stearothermophilus L-arabinose isomease Geobacillus stearothermophilus
5.3.1.4 GSAI 152 five mutations Geobacillus stearothermophilus
5.3.1.4 GSAI 153 three mutations Geobacillus stearothermophilus
5.3.1.4 L-arabinose aldose-ketose-isomerase
-
 Geobacillus stearothermophilus
5.3.1.4 L-arabinose isomerase
-
 Geobacillus stearothermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.3.1.4 7.5
-
 Q408V mutant enzyme with higher isomerization activites than the wild type enzyme Geobacillus stearothermophilus
5.3.1.4 7.5
-
 R408V mutant enzyme with higher isomerization activites than the wild type enzyme Geobacillus stearothermophilus
5.3.1.4 8.5
-
 wild type enzyme Geobacillus stearothermophilus