Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.22.28 extracted from

  • Dial, C.N.; Tate, P.M.; Kicmal, T.M.; Mounce, B.C.
    Coxsackievirus B3 responds to polyamine depletion via enhancement of 2A and 3C protease activity (2019), Viruses, 11, 403 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.28

Activating Compound

Activating Compound Comment Organism Structure
additional information polyamines facilitate viral protease activity Coxsackievirus B3

Protein Variants

Protein Variants Comment Organism
additional information generation of inactive mutant 3C52R through site-directed mutagenesis Coxsackievirus B3

Organism

Organism UniProt Comment Textmining
Coxsackievirus B3
-
 CVB3
-
Coxsackievirus B3 Nancy
-
 CVB3
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information the virus is passaged in Vero cells. Plaque size measurement Coxsackievirus B3
-

Synonyms

Synonyms Comment Organism
3C protease
-
 Coxsackievirus B3

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 in vivo assay at Coxsackievirus B3

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 in vivo assay at Coxsackievirus B3

General Information

General Information Comment Organism
malfunction CVB3 mutants, that arise with passage in polyamine-depleted conditions, contain mutations in the 2A protease (EC 3.4.22.29) and 3C protease (EC 3.4.22.28). These mutant proteases confer resistance to polyamine depletion. The 2A and 3C protease mutations also enhance reporter protease activity in polyamine-depleted conditions. The mutations promote cleavage of cellular eIF4G during infection of polyamine-depleted cells Coxsackievirus B3
physiological function viral proteases play many roles during infection, and picornaviruses encode two distinct proteases: 2A (2Apro) and 3C (3Cpro). The 2A and 3C picornaviral proteases function to cleave both host and viral proteins. 3C protease is responsible for the majority of viral polyprotein cleavage, while 2A facilitates the cleavage between the P1 and P2 protein segments. Polyamines are crucial to protease function during picornavirus infection Coxsackievirus B3