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Literature summary for 1.14.13.20 extracted from
- Self-assembled 2,4-dichlorophenol hydroxylase-inorganic hybrid nanoflowers with enhanced activity and stability (2018), RSC Adv., 8, 20976-20981 .
Application
| Application | Comment | Organism |
|---|---|---|
| degradation | immobilized enzyme exhibits great potential for application in bioremediation | uncultured bacterium |
| environmental protection | immobilized enzyme exhibits great potential for application in bioremediation | uncultured bacterium |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain DH5alpha | uncultured bacterium |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | synthesis of hybrid nanoflowers (hNFs) formed from cold-adapted 2,4-dichlorophenol hydroxylase (tfdBJLU) and Cu3(PO4)2 x 3H2O. Analysis of the influence of experimental factors, such as the pH of the solution mixture and the enzyme and Cu2+ concentrations, on the activity of the prepared tfdB-JLU-hNFs. 200 mM is the optimal Cu2+ concentration to get tfdB-JLU-hNFs with highest activity recovery, method optimization, overview. The tfdB-JLU-hNFs exhibit excellent durability with 58.34% residual activity after six successive cycles, and up to 90.58% residual activity after 20 days of storage. Comparison of storage stability of tfdB-JLU-hNFs and free tfdB-JLU at 1 mg/ml. This multistage and hierarchical flower-like structure can effectively increase enzyme activity and stability with respect to those of the free enzyme. The satisfactory removal rate of 2,4-dichlorophenol catalyzed by tfdB-JLU-hNFs suggests that this immobilized enzyme exhibits great potential for application in bioremediation | uncultured bacterium |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2,4-dichlorophenol + NADPH + H+ + O2 | uncultured bacterium | - |
3,5-dichlorocatechol + NADP+ + H2O | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| uncultured bacterium | - |
from soil | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain DH5alpha by nickel affinity chromatography and ultrafiltration | uncultured bacterium |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2,4-dichlorophenol + NADPH + H+ + O2 | - |
uncultured bacterium | 3,5-dichlorocatechol + NADP+ + H2O | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 2,4-DCP hydroxylase | - |
uncultured bacterium |
| 2,4-dichlorophenol hydroxylase | - |
uncultured bacterium |
| TfdB-JLU | - |
uncultured bacterium |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | uncultured bacterium |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | uncultured bacterium |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
uncultured bacterium | |
| NADPH | - |
uncultured bacterium | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | synthesis of hybrid nanoflowers (hNFs) formed from cold-adapted 2,4-dichlorophenol hydroxylase (tfdBJLU) and Cu3(PO4)2 x 3H2O. Analysis of the influence of experimental factors, such as the pH of the solution mixture and the enzyme and Cu2+ concentrations, on the activity of the prepared tfdB-JLU-hNFs. 200 mM is the optimal Cu2+ concentration to get tfdB-JLU-hNFs with highest activity recovery, method optimization, overview. The tfdB-JLU-hNFs exhibit excellent durability with 58.34% residual activity after six successive cycles, and up to 90.58% residual activity after 20 days of storage. This multistage and hierarchical flower-like structure can effectively increase enzyme activity and stability with respect to those of the free enzyme. The satisfactory removal rate of 2,4-dichlorophenol catalyzed by tfdB-JLU-hNFs suggests that this immobilized enzyme exhibits great potential for application in bioremediation | uncultured bacterium |
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