Cloned (Comment) | Organism |
---|---|
- |
Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of deletion mutants, i.e. expression of the N-terminal fragment residues 1-540, the N-terminal fragment residues 1-520, the N-terminal fragment residues 1-470, the N-terminal fragment residues 1-446, residues 1-520 with the deletion of the R3H domain, residues 1-446 with the deletion of the R3H domain. N-terminal fragment residues 1-446, residues 1-520 with the deletion of the R3H domain, residues 1-446 with the deletion of the R3H domain display 30.9%, 5.9% and 2.5% of the catalytic efficiency of the N-terminal fragment residues 1-520, respectively | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | O95453 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(A)6 + H2O | - |
Homo sapiens | 5'-AMP + ? | - |
? | |
poly(A) + H2O | average substrate length about 200 A | Homo sapiens | 5'-AMP + ? | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.65 | - |
Poly(A) | residues 1-446 with the deletion of the R3H domain, pH 7.0, temperature not specified in the publication | Homo sapiens | |
1.1 | - |
Poly(A) | residues 1-520 with the deletion of the R3H domain, pH 7.0, temperature not specified in the publication | Homo sapiens | |
5.6 | - |
Poly(A) | N-terminal fragment residues 1-446, pH 7.0, temperature not specified in the publication | Homo sapiens | |
7.6 | - |
Poly(A) | N-terminal fragment residues 1-520, pH 7.0, temperature not specified in the publication | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | the R3H domain has the ability to bind various oligonucleotides at the micromolar level with no oligo(A) specificity. The removal of the R3H domain dissociates poly(A)-specific ribonuclease into monomers, which still possess the RNA-binding ability and catalytic functions. The removal of the R3H domain does not affect the catalytic pattern of poly(A)-specific ribonuclease. Both R3H domain and RNA-recognition motif domain RRM may be essential for the high affinity of long poly(A) substrate, but the R3H domain does not contribute to the substrate recognition. Compared to the RRM domain, the R3H domain plays a more important role in the structural integrity of the dimeric poly(A)-specific ribonuclease | Homo sapiens |