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Literature summary for 3.4.22.B79 extracted from

  • Strauss, E.G.; De Groot, R.J.; Levinson, R.; Strauss, J.H.
    Identification of the active site residues in the nsP2 proteinase of Sindbis virus (1992), Virology, 191, 932-940.
    View publication on PubMed
Search for more literature for 3.4.22.B79

Protein Variants

Protein Variants Comment Organism
C481G mutation in C-terminal protease domain, abolishes catalytic activity, and is lethal Sindbis virus
C481R mutation in C-terminal protease domain, abolishes catalytic activity, and is lethal Sindbis virus
C481S mutation in C-terminal protease domain, abolishes catalytic activity, and is lethal Sindbis virus
C525R mutation in C-terminal protease domain, abolishes catalytic activity, and is lethal Sindbis virus
C525S mutant is active and processed normally Sindbis virus
H558A mutation in C-terminal protease domain, abolishes catalytic activity, and is lethal Sindbis virus
H558Q mutation in C-terminal protease domain, abolishes catalytic activity, and is lethal Sindbis virus
H558Y mutation in C-terminal protease domain, abolishes catalytic activity, and is lethal Sindbis virus
H619A mutant is active and processed normally Sindbis virus
H701A mutant is active and processed normally Sindbis virus
H709A mutant is active and processed normally Sindbis virus
H709R mutation in C-terminal protease domain, abolishes catalytic activity, and is lethal Sindbis virus
H709Y mutant is active and processed normally Sindbis virus
N561D mutant shows some activity, with normal processing Sindbis virus
N561S mutant shows some activity, with normal processing Sindbis virus
N609D mutant is active, almost no processing Sindbis virus
N609S mutant is active, with reduced processing Sindbis virus
N614D mutant shows enhanced processing, and is lethal Sindbis virus
N614S mutant shows some activity, with normal processing Sindbis virus
N693S mutant shows some activity, and is lethal Sindbis virus
S535T mutant is active and processed normally Sindbis virus
Y559A mutation in C-terminal protease domain, abolishes catalytic activity, and is lethal Sindbis virus

Organism

Organism UniProt Comment Textmining
Sindbis virus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the catalytic dyad is composed of Cys-481 and His-558 Sindbis virus ?
-
 ?
Sindbis virus core protein + H2O
-
 Sindbis virus Hydrolyzed Sindbis core protein
-
 ?

Synonyms

Synonyms Comment Organism
non-structural polyprotein 2
-
 Sindbis virus
nsP2
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 Sindbis virus