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Literature summary for 3.2.1.4 extracted from
- Identification of activity related amino acid mutations of a GH9 termite cellulase (2010), Biores. Technol., 101, 6438-6446.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence determination and comparison, expression of wild-type and mutant enzymes in Escherichia coli strain JM109 | Reticulitermes speratus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| A170S | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Reticulitermes speratus |
| A87S | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Reticulitermes speratus |
| D53X | site-directed mutagenesis, inactive mutant | Reticulitermes speratus |
| D56X | site-directed mutagenesis, inactive mutant | Reticulitermes speratus |
| E411X | site-directed mutagenesis, inactive mutant | Reticulitermes speratus |
| G147R | site-directed mutagenesis, inactive mutant | Reticulitermes speratus |
| G91A | site-directed mutagenesis, the mutant has 3-4fold higher activity towards carboxymethyl cellulose than the wild type enzyme | Reticulitermes speratus |
| G91A/K429A | site-directed mutagenesis, the double mutant has 7-13fold higher activity towards carboxymethyl cellulose than the wild type enzyme, the mutations show synegistic effects | Reticulitermes speratus |
| G91A/Y97W | site-directed mutagenesis, the double mutant has 7-13fold higher activity towards carboxymethyl cellulose than the wild type enzyme, the mutations show synegistic effects | Reticulitermes speratus |
| G91A/Y97W/G147R | site-directed mutagenesis, inactive mutant | Reticulitermes speratus |
| G91A/Y97W/K429A | site-directed mutagenesis, the triple mutant has 7-13fold higher activity towards carboxymethyl cellulose than the wild type enzyme, the mutations show synegistic effects | Reticulitermes speratus |
| G91I | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Reticulitermes speratus |
| I347V | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Reticulitermes speratus |
| K429A | site-directed mutagenesis, the mutant has 3-4fold higher activity towards carboxymethyl cellulose than the wild type enzyme | Reticulitermes speratus |
| L103I | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Reticulitermes speratus |
| N245S | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Reticulitermes speratus |
| N38D | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Reticulitermes speratus |
| Q202K | site-directed mutagenesis, almost inactive mutant | Reticulitermes speratus |
| Q42N/K43N | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Reticulitermes speratus |
| S173A | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Reticulitermes speratus |
| S25A | site-directed mutagenesis, almost inactive mutant | Reticulitermes speratus |
| S90D | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Reticulitermes speratus |
| Y329F | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Reticulitermes speratus |
| Y97F | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Reticulitermes speratus |
| Y97W | site-directed mutagenesis, the mutant has 3-4fold higher activity towards carboxymethyl cellulose than the wild type enzyme | Reticulitermes speratus |
| Y97W/K429A | site-directed mutagenesis, the double mutant has 7-13fold higher activity towards carboxymethyl cellulose than the wild type enzyme, the mutations show synegistic effects | Reticulitermes speratus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Reticulitermes speratus | - |
- |
- |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 109 | - |
purified recombinant mutant K429A | Reticulitermes speratus |
| 137 | - |
purified recombinant mutant G91A | Reticulitermes speratus |
| 154 | - |
purified recombinant mutant Y97W | Reticulitermes speratus |
| 248 | - |
purified recombinant mutant G91A/K429A | Reticulitermes speratus |
| 349 | - |
purified recombinant mutant G91A/Y97W | Reticulitermes speratus |
| 357 | - |
purified recombinant mutant Y97W/K429A | Reticulitermes speratus |
| 469 | - |
purified recombinant mutant G91A/Y97W/K429A | Reticulitermes speratus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| carboxymethyl cellulose + H2O | - |
Reticulitermes speratus | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| endo-beta-1,4-glucanase | - |
Reticulitermes speratus |
| GH9 termite cellulase | - |
Reticulitermes speratus |
| More | the enzyme belongs to the gylcosyl hydrolase family GH9 | Reticulitermes speratus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Reticulitermes speratus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 70 | - |
Reticulitermes speratus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | - |
assay at | Reticulitermes speratus |
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