Literature summary for 3.4.22.29 extracted from

Rivera, C.I.; Lloyd, R.E.
Modulation of enteroviral proteinase cleavage of poly(A)-binding protein (PABP) by conformation and PABP-associated factors (2008), Virology, 375, 59-72.

Search for more literature for 3.4.22.29

Activating Compound

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

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/ Products (Substrates)

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

Organism	UniProt	Comment	Textmining
coxsackievirus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
infected cell	-	coxsackievirus	-

Specific Activity [micromol/min/mg]

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 and Products (Substrate)

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

Synonyms	Comment	Organism
2A proteinase	-	coxsackievirus
2Apro	-	coxsackievirus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	coxsackievirus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	assay at	coxsackievirus

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Release 2023.1 (January 2023)