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3.4.21.114: equine arterivirus serine peptidase

This is an abbreviated version!
For detailed information about equine arterivirus serine peptidase, go to the full flat file.

Word Map on EC 3.4.21.114

Reaction

cleavage of (Glu/Gln)-/-(Gly/Ser/Ala) in arterivirus replicase translation products ORF1a and ORF1ab =

Synonyms

3C-like serine protease, 3CLSP, equine arteritis virus serine endopeptidase, non-structural protein 4, nonstructural protein 4, nsp4, nsp4 serine protease, nsp4SP, S32.001

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.114 equine arterivirus serine peptidase

Engineering

Engineering on EC 3.4.21.114 - equine arterivirus serine peptidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D1129E
mutant is able to cleave the Nsp4/5 site with wild-type efficiently but does not process the Nsp3/4 and Nsp5/6 junctions
D1129K
no Nsp3456 cleavage
D1129V
no Nsp3456 cleavage
H1103G
complete inhibition of Nsp3456 processing
H1103R
complete inhibition of Nsp3456 processing
H1198L
completely abolished processing of Nsp4/5 and Nsp5/6
H1198R
completely abolished processing of Nsp4/5 and Nsp5/6
H1198Y
completely abolished processing of Nsp4/5 and Nsp5/6
S1184C
mutation has no effect on Nsp3456 processing
S1184F
mutation has no effect on Nsp3456 processing
S1184I
S1184Y
mutation has no effect on Nsp3456 processing
T1179D
completely abolished processing of Nsp4/5 and Nsp5/6
T1179G
reduced cleavage of Nsp4/5, no cleavage of Nsp5/6 site
T1179N
retains wild-type activity towards Nsp4/5, cleaves Nsp5/6 with increased efficiency
T1179S
reduced cleavage of Nsp4/5, no cleavage of Nsp5/6 site
H1103G
-
complete inhibition of Nsp3456 processing
-
H1103R
-
complete inhibition of Nsp3456 processing
-
S1184C
-
mutation has no effect on Nsp3456 processing
-
S1184F
-
mutation has no effect on Nsp3456 processing
-
S1184I
-
mutation has no effect on Nsp3456 processing
-
D64A
site-directed mutagenesis, the mutant shows significantly reduced ability to induce apoptosis compared to the wild-type enzyme
H39A
site-directed mutagenesis, the mutant shows significantly reduced ability to induce apoptosis compared to the wild-type enzyme
S118A