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Literature summary extracted from

  • Kim, H.J.; Kim, J.H.; Oh, H.J.; Oh, D.K.
    Characterization of a mutated Geobacillus stearothermophilus L-arabinose isomerase that increases the production rate of D-tagatose (2006), J. Appl. Microbiol., 101, 213-221.
    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, the D-tagatose yield from the mutated enzyme is higher than from the wild type Geobacillus stearothermophilus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.1.4 expression in Escherichia coli of wild type and gali 153 mutant enzyme Geobacillus stearothermophilus

Protein Variants

EC Number Protein Variants Comment Organism
5.3.1.4 M322V/S393T/V408A error prone PCR mutagenesis using gali 152 as template, gali 153 with changes in 3 amino acids revealed a higher activity than gali 152 Geobacillus stearothermophilus

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.3.1.4 Cu2+
-
 Geobacillus stearothermophilus
5.3.1.4 Dulcitol weak inhibitor Geobacillus stearothermophilus
5.3.1.4 erythritol weak inhibitor Geobacillus stearothermophilus
5.3.1.4 L-arabitol strong inhibitory Geobacillus stearothermophilus
5.3.1.4 ribitol strong inhibitory Geobacillus stearothermophilus
5.3.1.4 xylitol weak inhibitor Geobacillus stearothermophilus
5.3.1.4 Zn2+
-
 Geobacillus stearothermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.3.1.4 67
-
 L-arabinose wild type enzyme Geobacillus stearothermophilus
5.3.1.4 100
-
 L-arabinose mutated enzyme Geobacillus stearothermophilus
5.3.1.4 145
-
 D-galactose wild type enzyme Geobacillus stearothermophilus
5.3.1.4 578
-
 D-galactose mutated enzyme Geobacillus stearothermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.3.1.4 Ba2+ activating Geobacillus stearothermophilus
5.3.1.4 Ca2+ activating Geobacillus stearothermophilus
5.3.1.4 Co2+ activating, highest activity of the mutated enzyme at 1.0 mM Geobacillus stearothermophilus
5.3.1.4 Cu2+ inhibitory Geobacillus stearothermophilus
5.3.1.4 Fe2+ activating Geobacillus stearothermophilus
5.3.1.4 Mg2+ activating Geobacillus stearothermophilus
5.3.1.4 Mn2+ activating, highest activity of the wild type enzyme at 1.0 mM Geobacillus stearothermophilus
5.3.1.4 Mo2+ activating Geobacillus stearothermophilus
5.3.1.4 Zn2+ inhibitory 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
-
-
5.3.1.4 Geobacillus stearothermophilus KCCM12265 Q9S467
-
-

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 2.3
-
 of the recombinant wild type enzyme after purification 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 D-galactose
-
 Geobacillus stearothermophilus KCCM12265 D-tagatose
-
 ?
5.3.1.4 L-arabinose other aldoses like D-fucose, D-ribose, D-allose, D-mannose and D-xylose are poor substrates for the wild type and the mutated enzymes Geobacillus stearothermophilus L-ribulose
-
 ?
5.3.1.4 L-arabinose other aldoses like D-fucose, D-ribose, D-allose, D-mannose and D-xylose are poor substrates for the wild type and the mutated enzymes Geobacillus stearothermophilus KCCM12265 L-ribulose
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.3.1.4 D-galactose isomerase
-
 Geobacillus stearothermophilus
5.3.1.4 gali 152 mutated L-arabinose isomerase from pL152 gene Geobacillus stearothermophilus
5.3.1.4 gali 153 mutated L-arabinose isomerase from pL153 gene Geobacillus stearothermophilus
5.3.1.4 L-arabinose aldose-ketose-isomerase
-
 Geobacillus stearothermophilus
5.3.1.4 L-arabinose isomerase
-
 Geobacillus stearothermophilus
5.3.1.4 pL 151
-
 Geobacillus stearothermophilus
5.3.1.4 pL 152
-
 Geobacillus stearothermophilus
5.3.1.4 pL 153
-
 Geobacillus stearothermophilus
5.3.1.4 pL151
-
 Geobacillus stearothermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.3.1.4 60
-
 wild type enzyme Geobacillus stearothermophilus
5.3.1.4 65
-
 mutated enzyme gali 153 Geobacillus stearothermophilus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
5.3.1.4 55 75
-
 Geobacillus stearothermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.3.1.4 8
-
 wild type and mutated enzyme Geobacillus stearothermophilus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
5.3.1.4 6.5 8.5
-
 Geobacillus stearothermophilus