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Literature summary for 3.4.22.66 extracted from

  • Oka, T.; Yamamoto, M.; Yokoyama, M.; Ogawa, S.; Hansman, G.S.; Katayama, K.; Miyashita, K.; Takagi, H.; Tohya, Y.; Sato, H.; Takeda, N.
    Highly conserved configuration of catalytic amino acid residues among calicivirus-encoded proteases (2007), J. Virol., 81, 6798-6806.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.66

Cloned(Commentary)

Cloned (Comment) Organism
-
 Sapovirus
-
 feline calicivirus

Organism

Organism UniProt Comment Textmining
feline calicivirus
-
-
-
Sapovirus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information four amino acid residues are essential to protease activities: H31, E52, C116, and H131. These amino acids are involved in the formation of a conserved catalytic surface Sapovirus ?
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 ?
additional information four amino acid residues are essential to protease activities: H39, E60, C122, and H137. These amino acids are involved in the formation of a conserved catalytic surface feline calicivirus ?
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 ?