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Literature summary extracted from
- Probing the molecular determinant for the catalytic efficiency of L-arabinose isomerase from Bacillus licheniformis (2010), Appl. Environ. Microbiol., 76, 1653-1660.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.3.1.4 | expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Bacillus licheniformis |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.3.1.4 | I370A | site-directed mutagenesis, the mutant catalytic activity is similar to the wild-type enzyme | Bacillus licheniformis |
| 5.3.1.4 | L345A | site-directed mutagenesis, the mutant catalytic activity is similar to the wild-type enzyme | Bacillus licheniformis |
| 5.3.1.4 | M185A | site-directed mutagenesis, the mutant catalytic activity is similar to the wild-type enzyme | Bacillus licheniformis |
| 5.3.1.4 | M349A | site-directed mutagenesis, the mutant catalytic activity is similar to the wild-type enzyme | Bacillus licheniformis |
| 5.3.1.4 | T276A | site-directed mutagenesis, the mutant catalytic activity is similar to the wild-type enzyme | Bacillus licheniformis |
| 5.3.1.4 | W439A | site-directed mutagenesis, the mutant catalytic activity is similar to the wild-type enzyme | Bacillus licheniformis |
| 5.3.1.4 | Y333A | site-directed mutagenesis, the catalytic site mutant shows 97.2% reduced activity compared to the wild-type enzyme | Bacillus licheniformis |
| 5.3.1.4 | Y333D | site-directed mutagenesis, the catalytic site mutant shows no activity | Bacillus licheniformis |
| 5.3.1.4 | Y333E | site-directed mutagenesis, the catalytic site mutant shows no activity | Bacillus licheniformis |
| 5.3.1.4 | Y333I | site-directed mutagenesis, the catalytic site mutant shows 72% reduced activity compared to the wild-type enzyme | Bacillus licheniformis |
| 5.3.1.4 | Y333K | site-directed mutagenesis, the catalytic site mutant shows no activity | Bacillus licheniformis |
| 5.3.1.4 | Y333V | site-directed mutagenesis, the catalytic site mutant shows 82% reduced activity compared to the wild-type enzyme | Bacillus licheniformis |
| 5.3.1.4 | Y333X | replacing Y333 with the aromatic amino acid Phe does not alter catalytic efficiency toward L-arabinose. In contrast, the activities of mutants containing a hydrophobic amino acid, Ala, Val, or Leu, decrease as the size of the hydrophobic side chain of the amino acid decreases. However, mutants containing hydrophilic and charged amino acids, such as Asp, Glu, and Lys, show almost no activity with L-arabinose | Bacillus licheniformis |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.3.1.4 | 8 | 16 | L-arabinose | pH 7.5, 50°C, recombinant mutant Y333V | Bacillus licheniformis |  |
| 5.3.1.4 | 369 | - |
L-arabinose | pH 7.5, 50°C, recombinant wild-type enzyme | Bacillus licheniformis | |
| 5.3.1.4 | 492 | - |
L-arabinose | pH 7.5, 50°C, recombinant mutant Y333F | Bacillus licheniformis | |
| 5.3.1.4 | 620 | - |
L-arabinose | pH 7.5, 50°C, recombinant mutant Y333W | Bacillus licheniformis | |
| 5.3.1.4 | 750 | - |
L-arabinose | pH 7.5, 50°C, recombinant mutant Y333I | Bacillus licheniformis | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.3.1.4 | Mn2+ | - |
Bacillus licheniformis | |
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 licheniformis | - |
L-ribulose | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.3.1.4 | Bacillus licheniformis | Q65J10 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.3.1.4 | recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Bacillus licheniformis |
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 | 3 | - |
purified recombinant mutant Y333A | Bacillus licheniformis |
| 5.3.1.4 | 18 | - |
recombinant purified mutant Y333V | Bacillus licheniformis |
| 5.3.1.4 | 28 | - |
recombinant purified mutant Y333I | Bacillus licheniformis |
| 5.3.1.4 | 105 | - |
purified recombinant wild-type enzyme | Bacillus licheniformis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.1.4 | L-arabinose | - |
Bacillus licheniformis | L-ribulose | - |
? | |
| 5.3.1.4 | L-arabinose | the Bacillus licheniformis L-arabinose isomerase shows a high degree of substrate specificity for L-arabinose. The conserved amino acid Y333 in the substrate binding pocket of the wild-type L-AI is important for the catalytic efficiency, other putative catalytic residues are E306, E333, H350, and H450 | Bacillus licheniformis | L-ribulose | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.3.1.4 | More | three-dimensional homology models of the wild-type and mutant enzyme proteins from crystal structure, PDB ID 2ajtA, overview | Bacillus licheniformis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.3.1.4 | L-AI | - |
Bacillus licheniformis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.3.1.4 | 50 | - |
assay at | Bacillus licheniformis |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.3.1.4 | 38.9 | - |
L-arabinose | pH 7.5, 50°C, recombinant mutant Y333V | Bacillus licheniformis | |
| 5.3.1.4 | 50.3 | - |
L-arabinose | pH 7.5, 50°C, recombinant mutant Y333I | Bacillus licheniformis | |
| 5.3.1.4 | 148.8 | - |
L-arabinose | pH 7.5, 50°C, recombinant mutant Y333W | Bacillus licheniformis | |
| 5.3.1.4 | 188.2 | - |
L-arabinose | pH 7.5, 50°C, recombinant mutant Y333F | Bacillus licheniformis | |
| 5.3.1.4 | 207.5 | - |
L-arabinose | pH 7.5, 50°C, recombinant wild-type enzyme | Bacillus licheniformis | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.3.1.4 | 7.5 | - |
assay at | Bacillus licheniformis |
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 | 0.048 | - |
L-arabinose | pH 7.5, 50°C, recombinant mutant Y333V | Bacillus licheniformis | |
| 5.3.1.4 | 0.067 | - |
L-arabinose | pH 7.5, 50°C, recombinant mutant Y333I | Bacillus licheniformis | |
| 5.3.1.4 | 0.24 | - |
L-arabinose | pH 7.5, 50°C, recombinant mutant Y333W | Bacillus licheniformis | |
| 5.3.1.4 | 0.38 | - |
L-arabinose | pH 7.5, 50°C, recombinant mutant Y333F | Bacillus licheniformis | |
| 5.3.1.4 | 0.56 | - |
L-arabinose | pH 7.5, 50°C, recombinant wild-type enzyme | Bacillus licheniformis | |
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