Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Penicillium crustosum |
Crystallization (Comment) | Organism |
---|---|
molecular modeling of the catalytic domain. The domain structurally belongs to the GH-A family | Penicillium crustosum |
Protein Variants | Comment | Organism |
---|---|---|
additional information | both the full-length enzyme and the catalytic domain have carboxymethylcellulase and filter paper hydrolase activity . The catalytic domain can also bind the cellulose substrate. The aromatic amino acids at the bottom of the barrel fold and those adjacent to the catalytic site significantly affect the cellulolytic activity and the cellulose binding affinity of the catalytic domain | Penicillium crustosum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
carboxymethylcellulose | Km value 9.2 mg/ml for full-length protein, 11.5 mG/ml for catalytic domain, respectively, pH 7.0, 45°C | Penicillium crustosum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Penicillium crustosum | U6A8H3 | - |
- |
Penicillium crustosum 601 | U6A8H3 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
carboxymethylcellulose + H2O | - |
Penicillium crustosum | ? | - |
? | |
carboxymethylcellulose + H2O | - |
Penicillium crustosum 601 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Egl1 | - |
Penicillium crustosum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
45 | - |
- |
Penicillium crustosum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
- |
Penicillium crustosum |