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Literature summary for 5.3.1.4 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

Application Comment Organism
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)

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

Protein Variants

Protein Variants Comment Organism
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

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

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus Q9S467
-
-
Geobacillus stearothermophilus KCCM12265 Q9S467
-
-

Purification (Commentary)

Purification (Comment) Organism
of the recombinant wild type and mutant enzymes Geobacillus stearothermophilus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3
-
of the recombinant wild type enzyme after purification Geobacillus stearothermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-galactose
-
Geobacillus stearothermophilus D-tagatose
-
?
D-galactose
-
Geobacillus stearothermophilus KCCM12265 D-tagatose
-
?
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
-
?
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

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

Temperature Optimum [°C]

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

Temperature Range [°C]

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

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
6.5 8.5
-
Geobacillus stearothermophilus