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Literature summary for 1.10.3.2 extracted from
- Protein engineering of laccase to enhance its activity and stability in the presence of organic solvents (2014), Eng. Life Sci., 14, 442-448 .
No PubMed abstract available
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E188A | in comparison with the wild type, the mutant enzyme shows an increase in Km value and a decrease in kcat. In comparison with the wild type, the mutant enzyme shows increased stability to organis solvents (ethanol, methanol, 1-propanol) | Bacillus sp. (in: Bacteria) |
| E188I | in comparison with the wild type, the mutant enzyme shows an increase in kcat and catalytic efficiency values and a decrease in Km. In comparison with the wild type, the mutant enzyme shows increased stability to organis solvents (ethanol, methanol, 1-propanol) | Bacillus sp. (in: Bacteria) |
| E188K | in comparison with the wild type, the mutant enzyme shows an increase in Km value and a decrease in kcat. In comparison with the wild type, the mutant enzyme shows increased stability to organis solvents (ethanol, methanol, 1-propanol) | Bacillus sp. (in: Bacteria) |
| E188L | in comparison with the wild type, the mutant enzyme shows an increase in kcat and catalytic efficiency values and a decrease in Km. In comparison with the wild type, the mutant enzyme shows increased stability to organis solvents (ethanol, methanol, 1-propanol) | Bacillus sp. (in: Bacteria) |
| E188R | in comparison with the wild type, the mutant enzyme shows an increase in kcat and catalytic efficiency values and a decrease in Km, In comparison with the wild type, the mutant enzyme shows increased stability to organis solvents (ethanol, methanol, 1-propanol) | Bacillus sp. (in: Bacteria) |
| E188V | in comparison with the wild type, the mutant enzyme shows an increase in kcat and catalytic efficiency values and a decrease in Km. In comparison with the wild type, the mutant enzyme shows increased stability to organis solvents (ethanol, methanol, 1-propanol) | Bacillus sp. (in: Bacteria) |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.1107 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, mutant enzyme E188R, in aqueous solution | Bacillus sp. (in: Bacteria) |  |
| 0.1151 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, mutant enzyme E188I, in aqueous solution | Bacillus sp. (in: Bacteria) | |
| 0.129 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, mutant enzyme E188L, in aqueous solution | Bacillus sp. (in: Bacteria) | |
| 0.1329 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, mutant enzyme E188V, in aqueous solution | Bacillus sp. (in: Bacteria) | |
| 0.1419 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, wild-type enzyme, in aqueous solution | Bacillus sp. (in: Bacteria) | |
| 0.1511 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, mutant enzyme E188K, in aqueous solution | Bacillus sp. (in: Bacteria) | |
| 0.1714 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, mutant enzyme E188A, in aqueous solution | Bacillus sp. (in: Bacteria) | |
Organic Solvent Stability
| Organic Solvent | Comment | Organism |
|---|---|---|
| 1-propanol | 9% (v/v), 50% of activity of wild-type enzyme remains. The stability of laccase in organic solvents is improved by introducing nonpolar (E188: A, I, L, and V) and positively charged (E188: K and R) residues in this region by site-directed mutagenesis. All variants show higher C50 values when compared to the wild type. Nonpolar amino acid substitutions are found to be the most efficient mutants for their remarkable increase in C50 value and a decrease in thermoinactivation rate in the presence of solvent. Replacing a negative residue with hydrophobic residues on the surface of a protein can enhance thermoresistance as well as solvent stability. The stability of the resulting enzymes is dependent on the length of the alkyl chain | Bacillus sp. (in: Bacteria) |
| Ethanol | 25% (v/v), 50% of activity of wild-type enzyme remains. The stability of laccase in organic solvents is improved by introducing nonpolar (E188: A, I, L, and V) and positively charged (E188: K and R) residues in this region by site-directed mutagenesis. All variants show higher C50 values when compared to the wild type. Nonpolar amino acid substitutions are found to be the most efficient mutants for their remarkable increase in C50 value and a decrease in thermoinactivation rate in the presence of solvent. Replacing a negative residue with hydrophobic residues on the surface of a protein can enhance thermoresistance as well as solvent stability. The stability of the resulting enzymes is dependent on the length of the alkyl chain | Bacillus sp. (in: Bacteria) |
| Methanol | 18% (v/v), 50% of activity of wild-type enzyme remains. The stability of laccase in organic solvents is improved by introducing nonpolar (E188: A, I, L, and V) and positively charged (E188: K and R) residues in this region by site-directed mutagenesis. All variants show higher C50 values when compared to the wild type. Nonpolar amino acid substitutions are found to be the most efficient mutants for their remarkable increase in C50 value and a decrease in thermoinactivation rate in the presence of solvent. Replacing a negative residue with hydrophobic residues on the surface of a protein can enhance thermoresistance as well as solvent stability. The stability of the resulting enzymes is dependent on the length of the alkyl chain | Bacillus sp. (in: Bacteria) |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus sp. (in: Bacteria) | B9W2C5 | - |
- |
| Bacillus sp. (in: Bacteria) HR03 | B9W2C5 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Bacillus sp. (in: Bacteria) |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2 | - |
Bacillus sp. (in: Bacteria) | ? | - |
? | |
| 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2 | - |
Bacillus sp. (in: Bacteria) HR03 | ? | - |
? | |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 21.2 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, mutant enzyme E188A, in aqueous solution | Bacillus sp. (in: Bacteria) | |
| 31.11 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, mutant enzyme E188K, in aqueous solution | Bacillus sp. (in: Bacteria) | |
| 45.8 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, wild-type enzyme, in aqueous solution | Bacillus sp. (in: Bacteria) | |
| 86.4 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, mutant enzyme E188L, in aqueous solution | Bacillus sp. (in: Bacteria) | |
| 98.2 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, mutant enzyme E188R, in aqueous solution | Bacillus sp. (in: Bacteria) | |
| 99.5 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, mutant enzyme E188V, in aqueous solution | Bacillus sp. (in: Bacteria) | |
| 102.8 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, mutant enzyme E188I, in aqueous solution | Bacillus sp. (in: Bacteria) | |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 120 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, mutant enzyme E188A, in aqueous solution | Bacillus sp. (in: Bacteria) | |
| 210 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, mutant enzyme E188K, in aqueous solution | Bacillus sp. (in: Bacteria) | |
| 322 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, wild-type enzyme, in aqueous solution | Bacillus sp. (in: Bacteria) | |
| 670 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, mutant enzyme E188L, in aqueous solution | Bacillus sp. (in: Bacteria) | |
| 750 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, mutant enzyme E188V, in aqueous solution | Bacillus sp. (in: Bacteria) | |
| 890 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, mutant enzyme E188I, in aqueous solution | Bacillus sp. (in: Bacteria) | |
| 900 | - |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) | pH 4.0, 22°C, mutant enzyme E188R, in aqueous solution | Bacillus sp. (in: Bacteria) | |
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