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

BRENDA support

Literature summary extracted from

  • Miyashita, K.; Okunishi, J.; Utsumi, R.; Komano, T.; Tamura, T.; Satoh, N.
    Cleavage specificity of coxsackievirus 3C proteinase for peptide substrate (1996), Biosci. Biotechnol. Biochem., 60, 705-707.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.28 coxsackievirus
-
-
-
3.4.22.28 coxsackievirus
-
 recombinant enzyme
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.28 acetyl-Glu-Ala-Leu-Phe-Gln-Gly-Gly-NH2 + H2O as good as acetyl-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Pro-Val coxsackievirus acetyl-Glu-Ala-Leu-Phe-Gln + Gly-Gly-NH2
-
 ?
3.4.22.28 acetyl-Glu-Ala-Leu-Phe-Gln-Gly-NH2 + H2O
-
 coxsackievirus acetyl-Glu-Ala-Leu-Phe-Gln + Gly-NH2
-
 ?
3.4.22.28 acetyl-Glu-Ala-Leu-Phe-Gln-Gly-Pro-NH2 + H2O
-
 coxsackievirus acetyl-Glu-Ala-Leu-Phe-Gln + Gly-Pro-NH2
-
 ?
3.4.22.28 acetyl-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Pro-Val + H2O sequence corresponding to 2C/3A cleavage site of polyprotein coxsackievirus acetyl-Glu-Ala-Leu-Phe-Gln + Gly-Pro-Pro-Val
-
 ?
3.4.22.28 acetyl-Glu-Ala-Leu-Phe-Gln-NH2 + H2O cleavage with reduced but significant efficiency, better substrate than acetyl-Glu-Ala-Leu-Phe-Gln-Gly-NH2 coxsackievirus acetyl-Glu-Ala-Leu-Phe-Gln + NH3
-
 ?
3.4.22.28 additional information no hydrolysis of acetyl-Glu-Ala-Leu-Phe-Glu-Gly-Pro coxsackievirus ?
-
 ?