3.4.23.B13: proteinase P15
This is an abbreviated version!
For detailed information about proteinase P15, go to the full flat file.
Word Map on EC 3.4.23.B13
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3.4.23.B13
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inflammasome
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caspase-1
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lipopolysaccharide
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pyroptosis
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noncanonical
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casp11
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caspase-11-dependent
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nod-like
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wedelolactone
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guanylate-binding
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endotoxic
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caspase-11-deficient
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gsdmd
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legionella
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rodentium
- 3.4.23.B13
-
inflammasome
- caspase-1
- lipopolysaccharide
-
pyroptosis
-
noncanonical
-
casp11
-
caspase-11-dependent
-
nod-like
- wedelolactone
-
guanylate-binding
-
endotoxic
-
caspase-11-deficient
-
gsdmd
-
legionella
-
rodentium
Reaction
efficient cleavage of Ala-Thr-His-Glu-Val-Tyr-Phe(NO2)-Val-Arg-Lys-Ala, no cleavage with Ser, Arg or Glu at P1, Gly or Phe at P2, and Pro at P3. Specifically liberates the five major structural proteins from the common gag precursor, as well as reverse transcriptase and integrase from the gag-pol precursor =
Synonyms
15gag proteinase, MAV-PR, myeloblastosis associated virus proteinase, p15gag proteinase
ECTree
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Engineering
Engineering on EC 3.4.23.B13 - proteinase P15
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A100L/V104T/R105P/G106V/S107N
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5 key residues predicted to form part of the enzyme subsites S1, S2, and S3 are changed to the residues occupying a similar or identical position in the HIV-1 enzyme. At pH 6.0, the mutated enzyme exhibits more than one order of magnitude higher activity than the wild-type, for all peptide substrates tested. Catalytic efficiency (ratio of turnover number: Km-value) is much closer to that of HIV-1 protease than to the wild-type enzyme, regardless of the amino acid residue occuring in P1, P2 or p3 of the substrate series
A100L/V104T/R105P/G106V/S107N
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proteolytic activity of the mutant enzyme is higher than that of the wild-type enzyme. For Ala-Thr-His-Gln-Val-Tyr-Phe(NO2)-Val-Arg-Lys-Ala the parameter turnover-number/Km-value shows a 23fold increase, alteration of the specificity of the mutant enzyme towards that of HIV-1 protease
A100L/V104T/R105P/G106V/S107N
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the mutant with marked preference for HIC-derived peptide substrates does not cleave the HIV-1 polyprotein
A100L/V104T/R105P/G106V/S107N
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mutant enzyme shows increased proteolytic activity in vitro, mutant plasmid-transfected turkey fibroblasts display an unimpaired virus production in cell cultures. The mutant progeny virus is infectious and ist pattern of gag processing products appears identical to that of wild-type virus. The predominant morphology of mutant viral particles is altered