Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.3.1.4 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

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

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Geobacillus stearothermophilus

Protein Variants

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

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ is closely bound to the protein even after treatment with EDTA 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
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Synonyms

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