Activating Compound | Comment | Organism | Structure |
---|---|---|---|
dithiothreitol | higher reducing potential in the buffer activates partial cleavage of poly(A) binding protein by 2Apro, no effect on 2Apro-mediated cleavage of eIF4G | coxsackievirus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
eukaryotic release factor 3 | increasing concentrations of recombinant His-tagged eRF3 lead to partial inhibition of 2Apro-proteolytic cleavage of poly(A) binding protein that increases modestly | coxsackievirus | |
PABP-interacting protein 2 | The inhibitory effect exerts by PABP-interacting protein 2 is more pronounced on 2Apro, as the lesser concentrations of PABP-interacting protein 2 that leads to partial inhibition of poly(A) binding protein cleavage by 3Cpro results in complete inhibition of 2A-pro-directed cleavage of poly(A) binding protein. 2Apro cleavage is strongly inhibited by in non-ribosome fractions, 40S and 80S ribosomes and polysome fractions. | coxsackievirus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
eIF4GI + H2O | coxsackievirus | - |
fragments of eIF4GI | - |
? | |
poly(A) binding protein + H2O | coxsackievirus | contains 1 cleavage site for 2A proteinase within the proline-rich linker domain | fragments of poly(A) binding protein | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
coxsackievirus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
infected cell | - |
coxsackievirus | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
addition of increasing concentrations of PABP-interacting protein 1 do not affect 2Apro-mediated cleavage of poly(A) binding protein, at the highest concentration (3 microg) of PABP-interacting protein 1 tested, increasing concentrations of 2Apro (0.5-1.5 microg) lead to a dose-dependent increase in cleavage of poly(A) binding protein by 2Apro proteinase | coxsackievirus |
additional information | - |
cleavage kinetics analysis indicates that poly(A) binding protein exists in multiple conformations, some of which are resistant to 2Apro cleavage and can be modulated by reducing potential | coxsackievirus |
additional information | - |
poly(A) binding protein in a HeLa S10 lysate is also highly resistant to cleavage by 2Apro despite high 2Apro activity versus eIF4GI, the initial cleavage rate is very slow and remains constant for 60 min before slowing down further upon extended incubation. Extended incubation also reveals a biphasic cleavage profile, incubation of 2Apro with recombinant His-poly(A) binding protein results in relatively poor and variable cleavage ranging from 0-20%, this suggested that most purified protein usually exists in a conformation not suitable for 2Apro recognition and binding | coxsackievirus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
eIF4GI + H2O | - |
coxsackievirus | fragments of eIF4GI | - |
? | |
poly(A) binding protein + H2O | contains 1 cleavage site for 2A proteinase within the proline-rich linker domain | coxsackievirus | fragments of poly(A) binding protein | - |
? |
Synonyms | Comment | Organism |
---|---|---|
2A proteinase | - |
coxsackievirus |
2Apro | - |
coxsackievirus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | coxsackievirus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | coxsackievirus |