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Literature summary extracted from
- Characterization of an L-arabinose isomerase from Bacillus subtilis (2010), Appl. Microbiol. Biotechnol., 85, 1839-1847.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.3.1.4 | 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
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.3.1.4 | E305A | site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme | Bacillus subtilis |
| 5.3.1.4 | 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 |
| 5.3.1.4 | E330A | site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme | Bacillus subtilis |
| 5.3.1.4 | 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 |
| 5.3.1.4 | H347A | site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme | Bacillus subtilis |
| 5.3.1.4 | H446A | site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme | Bacillus subtilis |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.3.1.4 | Cu2+ | - |
Bacillus subtilis |  |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.3.1.4 | Mn2+ | required, 42% activation at 1 mM | Bacillus subtilis | |
| 5.3.1.4 | 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]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 5.3.1.4 | 56000 | - |
2 * 56000, recombinant His6-tagged wild-type enzyme, SDS-PAGE | Bacillus subtilis |
| 5.3.1.4 | 115000 | - |
recombinant His6-tagged wild-type enzyme, gel filtration | Bacillus subtilis |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.1.4 | 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 | |
| 5.3.1.4 | 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 | |
| 5.3.1.4 | 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 | |
| 5.3.1.4 | 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 | |
| 5.3.1.4 | 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 | |
| 5.3.1.4 | 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
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.3.1.4 | Bacillus subtilis | C7F8M0 | gene araA | - |
| 5.3.1.4 | Bacillus subtilis 168 | C7F8M0 | gene araA | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.3.1.4 | recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Bacillus subtilis |
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 | 262 | - |
purified recombinant enzyme | Bacillus subtilis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.1.4 | L-aldose | - |
Bacillus subtilis | ? | - |
? | |
| 5.3.1.4 | 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 | |
| 5.3.1.4 | L-arabinose | the enzyme shows high substrate specificity | Bacillus subtilis | L-ribulose | - |
r | |
| 5.3.1.4 | 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 | |
| 5.3.1.4 | 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 | |
| 5.3.1.4 | L-arabinose | the enzyme shows high substrate specificity | Bacillus subtilis 168 | L-ribulose | - |
r | |
| 5.3.1.4 | 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 | |
| 5.3.1.4 | 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 | |
| 5.3.1.4 | 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 | |
| 5.3.1.4 | 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 | ? | - |
? | |
| 5.3.1.4 | 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
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.3.1.4 | dimer | 2 * 56000, recombinant His6-tagged wild-type enzyme, SDS-PAGE | Bacillus subtilis |
| 5.3.1.4 | More | wild-type and mutant enzymes, homology modeling and substrate docking analysis, overview | Bacillus subtilis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.3.1.4 | L-AI | - |
Bacillus subtilis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.3.1.4 | 32 | - |
- |
Bacillus subtilis |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.3.1.4 | 241.7 | - |
L-ribulose | pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme | Bacillus subtilis | |
| 5.3.1.4 | 241.7 | - |
L-aldose | pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme | Bacillus subtilis | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.3.1.4 | 7.5 | - |
- |
Bacillus subtilis |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.3.1.4 | 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 |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 5.3.1.4 | Bacillus subtilis | isoelectric focusing | - |
4.9 |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.3.1.4 | 2.02 | - |
L-ribulose | pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme | Bacillus subtilis | |
| 5.3.1.4 | 2.02 | - |
L-aldose | pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme | Bacillus subtilis | |
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