EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.6.1.18 | G38K | the mutant is more basic and interacts more strongly with the acidic membrane of cancer cells compared to the wild-type enzyme | Bos taurus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
4.6.1.18 | RNase inhibitor | RNase A, like most monomeric RNases, is strongly bound and inactivated in mammalian cells by the RNase inhibitor | Bos taurus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.6.1.18 | Bos taurus | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
4.6.1.18 | pancreas | - |
Bos taurus | - |
4.6.1.18 | semen | - |
Bos taurus | - |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.6.1.18 | dimer | constituted by two identical subunits covalently bound through two antiparallel disulfide bridges | Bos taurus |
4.6.1.18 | monomer | - |
Bos taurus |
4.6.1.18 | More | native RNase A can be induced to form various N- or C-terminal domain-swapped dimers, trimers, and larger oligomers, all reconstituting the active site and augmenting the enzymatic activity against dsRNA with respect to the native monomer. RNase A oligomers can also acquire cytotoxic activity both in vitro and in vivo | Bos taurus |
4.6.1.18 | oligomer | the enzyme can oligomerize through the 3D domain swapping of both N- and C-termini, and its multimers is enzymatically and biologically more active than the native dimer | Bos taurus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.6.1.18 | bovine seminal RNase | - |
Bos taurus |
4.6.1.18 | BS-RNase | - |
Bos taurus |
4.6.1.18 | RNase A | - |
Bos taurus |
4.6.1.18 | Seminal RNase | - |
Bos taurus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.6.1.18 | 37 | - |
assay at | Bos taurus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.6.1.18 | 7.4 | - |
assay at | Bos taurus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
4.6.1.18 | evolution | the enzyme belongs to the pancreatic-type secretory ribonuclease superfamily | Bos taurus |
4.6.1.18 | evolution | the enzyme belongs to the pancreatic-type secretory ribonuclease superfamily as a unique natively dimeric member | Bos taurus |
4.6.1.18 | physiological function | the enzyme has almost no anti-tumoral property in pancreatic adenocarcinoma cell lines and in nontumorigenic cells as normal control, and is largely ineffective as anti-proliferative and pro-apoptotic agent | Bos taurus |
4.6.1.18 | physiological function | the enzyme has good anti-tumoral property in pancreatic adenocarcinoma cell lines and in nontumorigenic cells as normal control, it stimulates a strong anti-proliferative and pro-apoptotic effect in cancer cells. The enzyme triggers Beclin1-mediated autophagic cancer cell death, providing evidence that high proliferation rate of cancer cells may render them more susceptible to autophagy by treatment with the enzyme | Bos taurus |