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Literature summary for 3.4.22.46 extracted from

  • Guarne, A.; Hampoelz, B.; Glaser, W.; Carpena, X.; Torma, J.; Fita, I.; Skern, T.
    Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes (2000), J. Mol. Biol., 302, 1227-1240.
    View publication on PubMed
Search for more literature for 3.4.22.46

Cloned(Commentary)

Cloned (Comment) Organism
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 Foot-and-mouth disease virus

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of LbproC51A, LbproC51A/C133S, sLbproC51A/C133S Foot-and-mouth disease virus

Inhibitors

Inhibitors Comment Organism Structure
additional information sensitive to high ionic strength, 50% inactivation by 20 mM NaCl or 10 mM CaCl2 Foot-and-mouth disease virus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0227
-
 Val-Gln-Arg-Lys-Leu-Lys-4-methylcoumarin 7-amide
-
 Foot-and-mouth disease virus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
foot-and-mouth disease leader protein + H2O Foot-and-mouth disease virus similar to other papain-like proteinases the enzyme possesses the catalytic cysteine and histidine residues, however the catalytic asparagine has been replaced by an aspartate. The interaction between the histidine and aspartate is exposed to solvent, as the tryptophan residues are missing. The cleavage site is between its own C-terminus and the N-terminus of VP4 ?
-
 ?
translation initiation factor eIF4G + H2O Foot-and-mouth disease virus
-
 additional information
-
 ?

Organism

Organism UniProt Comment Textmining
Foot-and-mouth disease virus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
foot-and-mouth disease leader protein + H2O similar to other papain-like proteinases the enzyme possesses the catalytic cysteine and histidine residues, however the catalytic asparagine has been replaced by an aspartate. The interaction between the histidine and aspartate is exposed to solvent, as the tryptophan residues are missing. The cleavage site is between its own C-terminus and the N-terminus of VP4 Foot-and-mouth disease virus ?
-
 ?
additional information no hydrolysis of Phe-Arg-4-methylcoumarin 7-amide, Val-Lue-Lys-4-methylcoumarin 7-amide, classical papain substrates, or Ser-Phe-Ala-Asn-Leu-Gly-4-methylcoumarin 7-amide, corresponding to the N-terminal portion of the eIF4G cleavage site Foot-and-mouth disease virus ?
-
 ?
translation initiation factor eIF4G + H2O
-
 Foot-and-mouth disease virus additional information
-
 ?
Val-Gln-Arg-Lys-Leu-Lys-4-methylcoumarin 7-amide + H2O the substrate corresponds to the six C-terminal amino acids of the leader protein Foot-and-mouth disease virus Val-Gln-Arg-Lys-Leu-Lys + 7-amino-4-methylcoumarin
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 substrate Val-Gln-Arg-Lys-Leu-Lys-4-methylcoumarin 7-amide Foot-and-mouth disease virus

pH Range

pH Minimum pH Maximum Comment Organism
7.2 9.8 less than 50% of maximal activity above and below, substrate Val-Gln-Arg-Lys-Leu-Lys-4-methylcoumarin 7-amide Foot-and-mouth disease virus