Cloned (Comment) | Organism |
---|---|
gene araA, DNA and amino acid sequence determination and analysis, His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Bacillus subtilis |
Protein Variants | Comment | Organism |
---|---|---|
E305A | site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme | Bacillus subtilis |
E305A | site-directed mutagenesis, mutation of the conserved catalytic residue leads to complete loss of catalytic activity, structure comparison to the wild-type enzyme | Bacillus subtilis |
E330A | site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme | Bacillus subtilis |
E330A | site-directed mutagenesis, mutation of the conserved catalytic residue leads to complete loss of catalytic activity, structure comparison to the wild-type enzyme | Bacillus subtilis |
H347A | site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme | Bacillus subtilis |
H446A | site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme | Bacillus subtilis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | - |
Bacillus subtilis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | required, 42% activation at 1 mM | Bacillus subtilis | |
additional information | the enzyme is not stimulated by Mg2+, Ca2+, Zn2+, Fe2+, or Ni2+ at 1 mM each, and is unaffected by EDTA at concentrations ranging from 1 to 10 mM | Bacillus subtilis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
56000 | - |
2 * 56000, recombinant His6-tagged wild-type enzyme, SDS-PAGE | Bacillus subtilis |
115000 | - |
recombinant His6-tagged wild-type enzyme, gel filtration | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-arabinose | Bacillus subtilis | L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of Larabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways | L-ribulose | - |
r | |
L-arabinose | Bacillus subtilis | L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways | L-ribulose | - |
r | |
L-arabinose | Bacillus subtilis 168 | L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of Larabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways | L-ribulose | - |
r | |
L-arabinose | Bacillus subtilis 168 | L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways | L-ribulose | - |
r | |
L-ribulose | Bacillus subtilis | L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways | L-arabinose | - |
r | |
L-ribulose | Bacillus subtilis 168 | L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways | L-arabinose | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | C7F8M0 | gene araA | - |
Bacillus subtilis 168 | C7F8M0 | gene araA | - |
Purification (Comment) | Organism |
---|---|
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Bacillus subtilis |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
262 | - |
purified recombinant enzyme | Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aldose | - |
Bacillus subtilis | ? | - |
? | |
L-arabinose | L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of Larabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways | Bacillus subtilis | L-ribulose | - |
r | |
L-arabinose | the enzyme shows high substrate specificity | Bacillus subtilis | L-ribulose | - |
r | |
L-arabinose | L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways | Bacillus subtilis | L-ribulose | - |
r | |
L-arabinose | L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of Larabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways | Bacillus subtilis 168 | L-ribulose | - |
r | |
L-arabinose | the enzyme shows high substrate specificity | Bacillus subtilis 168 | L-ribulose | - |
r | |
L-arabinose | L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways | Bacillus subtilis 168 | L-ribulose | - |
r | |
L-ribulose | L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways | Bacillus subtilis | L-arabinose | - |
r | |
L-ribulose | L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways | Bacillus subtilis 168 | L-arabinose | - |
r | |
additional information | no activity with L-ribose, L-xylose, D-galactose, D-mannose, and D-xylose. Wild-type and mutant enzymes, homology modeling and substrate docking analysis, overview | Bacillus subtilis | ? | - |
? | |
additional information | no activity with L-ribose, L-xylose, D-galactose, D-mannose, and D-xylose. Wild-type and mutant enzymes, homology modeling and substrate docking analysis, overview | Bacillus subtilis 168 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 56000, recombinant His6-tagged wild-type enzyme, SDS-PAGE | Bacillus subtilis |
More | wild-type and mutant enzymes, homology modeling and substrate docking analysis, overview | Bacillus subtilis |
Synonyms | Comment | Organism |
---|---|---|
L-AI | - |
Bacillus subtilis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
32 | - |
- |
Bacillus subtilis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
241.7 | - |
L-ribulose | pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme | Bacillus subtilis | |
241.7 | - |
L-aldose | pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme | Bacillus subtilis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
- |
Bacillus subtilis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 9 | 31%, 68%, 87%, and 48% of maximum activity at pH 6.0, pH 7.0, pH 8.0, and pH 9.0, respectively | Bacillus subtilis |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Bacillus subtilis | isoelectric focusing | - |
4.9 |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.02 | - |
L-ribulose | pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme | Bacillus subtilis | |
2.02 | - |
L-aldose | pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme | Bacillus subtilis |