Information on EC 3.4.22.B20 - PfpI endopeptidase

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The expected taxonomic range for this enzyme is: Pyrococcus furiosus

EC NUMBER
COMMENTARY hide
3.4.22.B20
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
PfpI endopeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
efficient cleavage of Ala-Ala-Phe-/-7-amido-4-methylcoumarinamide. Dominant protease in Pyrococcus furiosus
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ala-Ala-Phe-7-amido-4-methylcoumarin
Ala-Ala-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
Ala-Phe-Lys-7-amido-4-methylcoumarin
Ala-Phe-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
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-
-
-
?
azocasein + H2O
?
show the reaction diagram
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-
-
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?
Gelatin + H2O
?
show the reaction diagram
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-
-
-
?
Leu-Tyr-7-amido-4-methylcoumarin
Leu-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
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-
-
-
?
Suc-Ala-Ala-Phe-NHMec + H2O
Suc-Ala-Ala-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
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pH 7, NHMec = 7-amino-4-methylcoumaryl
NHMec = 7-amino-4-methylcoumaryl
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaCl
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100 mM, increases proteolytic activity by about 50%
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-lauryl sarcosine
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0.01% v/v, increases proteolytic activity by about 50%
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
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enzyme form PfpI-C1, reaction with Ala-Ala-Phe-7-amido-4-methylcoumarinamide
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2 - 8.5
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pH 5.2: about 60% of maximal activity, pH 8.5: about 50% of maximal activity, enzyme form PfpI-C1, reaction with Ala-Ala-Phe-7-amido-4-methylcoumarinamide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
84
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enzyme form PfpI-C1, reaction with Leu-Tyr-7-amido-4-methylcoumarinamide
95
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reaction with Ala-Ala-Phe-7-amido-4-methylcoumarinamide, recombinant enzyme
97
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enzyme form PfpI-C1, reaction with Ala-Phe-Lys-7-amido-4-methylcoumarinamide
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 110
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50C: about 55% of maximal activity, 110C: about 45% of maximal activity, enzyme form PfpI-C1, reaction with Ala-Ala-Phe-7-amido-4-methylcoumarinamide
70 - 100
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70C: about 70% of maximal activity, 100C: about 75% of maximal activity, reaction with Ala-Ala-Phe-7-amido-4-methylcoumarinamide, recombinant enzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.7 - 3.9
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trimer, experimentally determined
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66000
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after heating at 95C in 1% SDS for 24 h, SDS-PAGE
86000
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SDS-PAGE, the protein is not fully denatured by SDS
124000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x + 18800, homomultimer, SDS-PAGE
hexamer
trimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
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half life is 45 min, in presence of 0.5 M KHPO4 the half-life is extended to 80 min, activity with Ala-Ala-Phe-7-amido-4-methylcoumarinamide
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-mercaptoethanol
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the protease retains some proteolytic activity in the presence of 2-mercaptoethanol
dithiothreitol
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the protease retains some proteolytic activity in the presence of dithiothreitol
SDS
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the protease is resistant to SDS
urea
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the protease is resistant to urea
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purification of two enzyme forms: PfpI-C1 and PfpI-C2
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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