EC Number | Cloned (Comment) | Organism |
---|---|---|
3.1.21.1 | expression of wild-type and mutants in COS-7 cells | Bos taurus |
3.1.21.1 | expression of wild-type and mutants in COS-7 cells | Homo sapiens |
3.1.21.1 | expression of wild-type and mutants in COS-7 cells | Equus caballus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.1.21.1 | N106Q | enzyme activity is lower than that of the wild-type, is unstable to heat and less resistant to trypsin | Homo sapiens |
3.1.21.1 | N106Q | enzyme activity is lower than that of the wild-type, is unstable to heat and less resistant to trypsin | Equus caballus |
3.1.21.1 | N106Q | enzyme activity is lower than that of the wild-type, is unstable to heat, trypsin resistance is similar to that of the wild-type | Bos taurus |
3.1.21.1 | N18Q | enzyme activity is lower than that of the wild-type, is unstable to heat and less resistant to trypsin | Homo sapiens |
3.1.21.1 | N18Q | enzyme activity is lower than that of the wild-type, is unstable to heat and less resistant to trypsin | Equus caballus |
3.1.21.1 | N18Q | enzyme activity is lower than that of the wild-type, is unstable to heat, trypsin resistance is similar to that of the wild-type | Bos taurus |
3.1.21.1 | N18Q/N106Q | enzyme activity is lower than those of the single mutants, is unstable to heat and is the most sensitive to trypsin | Homo sapiens |
3.1.21.1 | N18Q/N106Q | enzyme activity is lower than those of the single mutants, is unstable to heat and is the most sensitive to trypsin | Equus caballus |
3.1.21.1 | N18Q/N106Q | enzyme activity is lower than those of the single mutants, is unstable to heat, trypsin resistance decreases in a time-dependent manner | Bos taurus |
EC Number | General Stability | Organism |
---|---|---|
3.1.21.1 | N18 and N106 are both necessary for full enzymatic activity, heat-stability, and trypsin resistance | Bos taurus |
3.1.21.1 | N18 and N106 are both necessary for full enzymatic activity, heat-stability, and trypsin resistance | Homo sapiens |
3.1.21.1 | N18 and N106 are both necessary for full enzymatic activity, heat-stability, and trypsin resistance | Equus caballus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.1.21.1 | additional information | is resistant to trypsin | Homo sapiens | |
3.1.21.1 | Trypsin | is less resistant to trypsin than human DNase I, DNase I activity decreases gradually | Bos taurus | |
3.1.21.1 | Trypsin | is less resistant to trypsin than human DNase I, DNase I activity decreases gradually | Equus caballus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.21.1 | Bos taurus | - |
- |
- |
3.1.21.1 | Equus caballus | Q4AEE3 | - |
- |
3.1.21.1 | Homo sapiens | P24855 | - |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.1.21.1 | additional information | pancreas-parotid | Bos taurus | - |
3.1.21.1 | pancreas | - |
Homo sapiens | - |
3.1.21.1 | parotid gland | - |
Equus caballus | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.21.1 | salmon testis DNA + H2O | - |
Bos taurus | 5'-phosphooligonucleotides + ? | - |
? | |
3.1.21.1 | salmon testis DNA + H2O | - |
Homo sapiens | 5'-phosphooligonucleotides + ? | - |
? | |
3.1.21.1 | salmon testis DNA + H2O | - |
Equus caballus | 5'-phosphooligonucleotides + ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.21.1 | deoxyribonuclease I | - |
Bos taurus |
3.1.21.1 | deoxyribonuclease I | - |
Homo sapiens |
3.1.21.1 | deoxyribonuclease I | - |
Equus caballus |
3.1.21.1 | DNase I | - |
Bos taurus |
3.1.21.1 | DNase I | - |
Homo sapiens |
3.1.21.1 | DNase I | - |
Equus caballus |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.21.1 | additional information | - |
both N-linked glycosylation sites N18 and N106 are required for heat stability | Bos taurus |
3.1.21.1 | additional information | - |
both N-linked glycosylation sites N18 and N106 are required for heat stability | Homo sapiens |
3.1.21.1 | additional information | - |
both N-linked glycosylation sites N18 and N106 are required for heat stability | Equus caballus |