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Literature summary for 3.1.1.3 extracted from
- Improved thermostability and the optimum temperature of Rhizopus arrhizus lipase by directed evolution (2006), J. Mol. Catal. B, 43, 33-39.
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| library screening, DNA and amino acid sequence determination and anaylsis, expression of wild-type and mutant enzymes in Pichia pastoris strain GS115 as secreted proteins, subcloning in Escherichia coli | Rhizopus arrhizus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| A9T | random mutagenesis, the mutation of residue A9 results in only marginally affected thermostability and optimum reaction temperature compared to the wild-type enzyme | Rhizopus arrhizus |
| A9T/E190V/M225I | random mutagenesis, the mutation of residues A9 and M225 result in only marginally affected thermostability and optimum reaction temperature compared to the wild-type enzyme, while the mutation of E190 is critical for thermostability and optimum reaction temperature | Rhizopus arrhizus |
| E190V | random mutagenesis, the mutation of E190 is critical for thermostability and optimum reaction temperature | Rhizopus arrhizus |
| M225I | random mutagenesis, the mutation of residues M225 result in only marginally affected thermostability and optimum reaction temperature compared to the wild-type enzyme | Rhizopus arrhizus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhizopus arrhizus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| secreted recombinant wild-type and mutant enzymes from Pichia pastoris strain GS115 by ultrafiltration, and dialysis, followed by anion exchange and hydrophobic interaction chromatography | Rhizopus arrhizus |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| triacylglycerol + H2O = diacylglycerol + a carboxylate | the catalytic center is formed by Ser145, Asp204, His257 | Rhizopus arrhizus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 2050 | - |
purified recombinant mutant enzyme | Rhizopus arrhizus |
| 2500 | - |
purified recombinant wild-type enzyme | Rhizopus arrhizus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| olive oil + H2O | - |
Rhizopus arrhizus | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| lipase | - |
Rhizopus arrhizus |
| RAL | - |
Rhizopus arrhizus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | - |
- |
Rhizopus arrhizus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 60 | mutant enzyme | Rhizopus arrhizus |
| 30 | 50 | wild-type enzyme | Rhizopus arrhizus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
the half-life of the purified recombinant wild-type enzyme is 7 min, for the mutant A9T/E190V/M225I 83 min, for mutant A9T 7 min, for mutant M225I 9 min, and for mutant E190V 76 min | Rhizopus arrhizus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Rhizopus arrhizus |
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Release 2023.1 (January 2023)
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