EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.73 | gene PtLic16A, DNA and amino acid sequence determination and analysis, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Paecilomyces sp. 'thermophila' |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.73 | C263S | random mutagenesis, the mutant shows an acidic shift in the pH optimum and altered substrate specificity compared to the wild-type enzyme | Paecilomyces sp. 'thermophila' |
3.2.1.73 | D221G2 | random mutagenesis, the mutant shows unaltered properties compared to the wild-type enzyme | Paecilomyces sp. 'thermophila' |
3.2.1.73 | D56G | random mutagenesis, the mutant shows an acidic shift in the pH optimum and altered substrate specificity compared to the wild-type enzyme | Paecilomyces sp. 'thermophila' |
3.2.1.73 | D56G/D221G/C263S | random mutagenesis, mutant PtLic16AM2 shows an acidic shift in the pH optimum and altered substrate specificity compared to the wild-type enzyme. Mutation D221G alone does not lead to altered enzyme properties | Paecilomyces sp. 'thermophila' |
3.2.1.73 | additional information | screening of the random mutant library, mutations D56G, D221G, and C263S have only minor effects on specific activity and pH stability | Paecilomyces sp. 'thermophila' |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.73 | additional information | - |
additional information | 3.69 mg/ml for the wild-type enzyme and 3.30 mg/ml for mutant D56G/D221G/C263S, with barley beta-glucan at pH 5.0, 70°C | Paecilomyces sp. 'thermophila' |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.2.1.73 | extracellular | - |
Paecilomyces sp. 'thermophila' | - |
- |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.73 | additional information | Paecilomyces sp. 'thermophila' | beta-1,3-1,4-glucanase strictly cleaves the beta-1,4-D-glucosidic bonds adjacent to beta-1,3-linkages in mixed linked beta-glucans | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.73 | Paecilomyces sp. 'thermophila' | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.1.73 | recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) | Paecilomyces sp. 'thermophila' |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.73 | barley beta-glucan + H2O | - |
Paecilomyces sp. 'thermophila' | ? | - |
? | |
3.2.1.73 | additional information | beta-1,3-1,4-glucanase strictly cleaves the beta-1,4-D-glucosidic bonds adjacent to beta-1,3-linkages in mixed linked beta-glucans | Paecilomyces sp. 'thermophila' | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.2.1.73 | More | molecular structure modeling and analysis | Paecilomyces sp. 'thermophila' |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.73 | beta-1,3-1,4-glucanase | - |
Paecilomyces sp. 'thermophila' |
3.2.1.73 | PtLic16A | - |
Paecilomyces sp. 'thermophila' |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.73 | 70 | - |
- |
Paecilomyces sp. 'thermophila' |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.73 | 40 | 90 | activity range, wild-type and mutant enzymes, profile overview | Paecilomyces sp. 'thermophila' |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.73 | 102 | - |
Barley beta-glucan | pH 5.0, 70°C, wild-type enzyme | Paecilomyces sp. 'thermophila' | |
3.2.1.73 | 143 | - |
Barley beta-glucan | pH 5.0, 70°C, mutant D56G/D221G/C263S | Paecilomyces sp. 'thermophila' |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.73 | additional information | - |
amino acid residues at positions 56 and 263 are important in determining optimal pH activity | Paecilomyces sp. 'thermophila' |
3.2.1.73 | 5 | - |
mutant D56G/D221G/C263S | Paecilomyces sp. 'thermophila' |
3.2.1.73 | 5.5 | - |
mutant C263S | Paecilomyces sp. 'thermophila' |
3.2.1.73 | 6 | - |
mutant D56G | Paecilomyces sp. 'thermophila' |
3.2.1.73 | 7 | - |
wild-type enzyme and mutant D221G | Paecilomyces sp. 'thermophila' |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.73 | 3 | 10 | activity range, wild-type and mutant enzymes, profile overview | Paecilomyces sp. 'thermophila' |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.2.1.73 | additional information | molecular structure modeling and analysis | Paecilomyces sp. 'thermophila' |