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Literature summary for 3.4.22.28 extracted from

  • Miyashita, K.; Kusumi, M.; Utsumi, R.; Katayama, S.; Noda, M.; Komano, T.; Satoh, N.
    Site-directed mutagenesis of the putative active site residues of 3C proteinase of coxsackievirus B3: evidence of a functional relationship with trypsin-like serine proteinases (1993), Protein Eng., 6, 189-193.
    View publication on PubMed
Search for more literature for 3.4.22.28

Cloned(Commentary)

Cloned (Comment) Organism
expression as a fusion protein in Escherichia coli coxsackievirus

Inhibitors

Inhibitors Comment Organism Structure
iodoacetamide only wild-type enzyme, not C147S-mutant coxsackievirus

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble recombinant enzyme coxsackievirus
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Organism

Organism UniProt Comment Textmining
coxsackievirus
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coxsackievirus
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 recombinant enzyme
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coxsackievirus
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 wild-type and catalytic site-directed mutants
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Glu-Ala-Leu-Phe-Gln-Gly-Pro-Pro-Val + H2O represents 2C/3A cleavage site, wild-type and C147S mutant, the latter with very reduced activity coxsackievirus Glu-Ala-Leu-Phe-Gln + Gly-Pro-Pro-Val
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 ?
additional information all catalytic-site mutations result in reduction or inactivation of autocatalytic cleavage of recombinant 3C precursor protein, Cys147 to Ala mutant is inactive, Cys147 to Ser has reduced in-cis and in-trans activity coxsackievirus ?
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 ?