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Literature summary extracted from
- Isomeric replacement of a single aspartic acid induces a marked change in protein function the example of ribonuclease A (2017), ACS Omega, 2, 260-267 .
No PubMed abstract available
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.6.1.18 | expression in Escherichia coli | Bos taurus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.6.1.18 | N121X | L-alpha-Asp at position 121 in RNase A is replaced by L-beta-, D-alpha-, and D-beta-Asp. The objective aspartic acid at position 121 is located near the active site and related to RNA cleavage. The RNase A with L-alpha-Asp at position 121 shows a normal activity. The catalytic activity of L-beta-, D-alpha-, and D-beta-Asp-containing RNase A is markedly decreased | Bos taurus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.6.1.18 | Bos taurus | P61823 | - |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.6.1.18 | ribonuclease A | - |
Bos taurus |
| 4.6.1.18 | RNase A | - |
Bos taurus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.6.1.18 | 25 | - |
assay at | Bos taurus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.6.1.18 | 7 | - |
assay at | Bos taurus |
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Release 2023.1 (January 2023)
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