Literature summary for 3.4.21.113 extracted from

Tautz, N.; Kaiser, A.; Thiel, H.J.
NS3 serine protease of bovine viral diarrhea virus: characterization of active site residues, NS4A cofactor domain, and protease-cofactor interactions (2000), Virology, 273, 351-363.

Search for more literature for 3.4.21.113

Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	the central region of NS4A represents the cofactor domain	Bovine viral diarrhea virus 1

Protein Variants

Protein Variants	Comment	Organism
D1686G	mutation does not induce obvious changes in processing	Bovine viral diarrhea virus 1
D1695A	mutation does not induce obvious changes in processing	Bovine viral diarrhea virus 1
additional information	the NS3 protease is sensitive to N-terminal truncation because a deletion of 6 amino acids significantly reduces the cleavage efficiency at the NS4A/4B site	Bovine viral diarrhea virus 1
S1752C	mutant enzyme exhibits only cleavage activity at the NS3/4A site	Bovine viral diarrhea virus 1
S1752T	mutant enzyme exhibits only cleavage activity at the NS3/4A site	Bovine viral diarrhea virus 1
S1752T	mutant enzyme still shows residual activity	Bovine viral diarrhea virus 1

Organism

Organism	UniProt	Comment	Textmining
Bovine viral diarrhea virus 1	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
bovine viral diarrhea virus polyprotein + H2O	cleavages leading to the release of NS4A, NS4B, NS5A, and NS5B	Bovine viral diarrhea virus 1	?	-	?
additional information	His1678, Asp1686 and Ser1752 constitute the catalytic triad	Bovine viral diarrhea virus 1	?	-	?

Synonyms

Synonyms	Comment	Organism
NS3 serine protease	-	Bovine viral diarrhea virus 1

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Release 2023.1 (January 2023)