Information on EC 3.4.21.103 - physarolisin

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.103
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RECOMMENDED NAME
GeneOntology No.
physarolisin
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Milk clotting activity. Preferential cleavage of Gly8-/-Ser in B chain of insulin most rapidly, followed by Leu11!Val, Cys(SO3H)19-/-Gly and Phe24-/-Phe. No action on Ac-Phe-Tyr(I)2.
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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aspartic endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY hide
94949-28-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
proteinase E, closely similar enzyme
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Manually annotated by BRENDA team
closely similar enzyme
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
azocasein + H2O
?
show the reaction diagram
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-
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bovine albumin + H2O
?
show the reaction diagram
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-
-
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casein + H2O
?
show the reaction diagram
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-
-
-
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Cytochrome c + H2O
?
show the reaction diagram
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-
-
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Glucagon + H2O
?
show the reaction diagram
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?
Hemoglobin + H2O
?
show the reaction diagram
Hemoglobin + H2O
Hydrolyzed hemoglobin
show the reaction diagram
hide powder azure + H2O
?
show the reaction diagram
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-
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histone + H2O
?
show the reaction diagram
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-
-
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insulin B chain + H2O
?
show the reaction diagram
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-
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?
KPIEFF(NO2)RL + H2O
?
show the reaction diagram
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-
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?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
show the reaction diagram
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Lys-Pro-Ile-Glu-Phe-(4-nitrophenyl)Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitrophenyl)Arg-Leu
show the reaction diagram
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?
ovalbumin + H2O
?
show the reaction diagram
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oxidized insulin B + H2O
?
show the reaction diagram
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?
oxidized insulin B chain + H2O
?
show the reaction diagram
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the major cleavage sites are Gly8-Ser9, Leu11-Val12, Cys19-Gly20, Gly20-Glu21, and Phe24-Phe25
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?
Oxidized insulin B-chain + H2O
Hydrolyzed insulin B-chain
show the reaction diagram
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major cleavage sites: Gly8-Ser9 (most susceptible), Leu11-Val12, Cysteic acid19-Gly20 and Phe24-Phe25
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Substance P + H2O
?
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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involved in general protein degradation within the lysosomes of Dictyostelium discoideum
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DAN
in the presence of cupric ions
Diazoacetyl-D,L-norleucine methyl ester
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in presence of Cu2+
Diazoacetyl-DL-norleucine methyl ester
diisopropyl fluorophosphate
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23% inhibition by 0.5 mM, 76% inhibition by 10 mM
Pepstatin
PMSF
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10 mM, 21% inhibition
SH-reagents
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tosyl-L-Leu-chloromethylketone
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10 mM, 18% inhibition
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 3
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hemoglobin, azocasein
2.5
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hide powder azure
4.2
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hydrolysis of oxidized insulin B chain
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.3 - 3
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pH 1.3: about 25% of activity maximum, pH 3.0: about 35% of activity maximum
3.7 - 5.3
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pH 3.7: about 40% of maximal actuvity, pH 5.3: about 35% of maximal activity, hydrolysis of oxidized insulin B chain
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 30
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3°C: about 50% of maximal activity, 30°C: about 60% of maximal activity, hydrolysis of oxidized insulin B chain
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58000
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x * 58000
68000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 9
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25°C, 24 h, stable
647478
2 - 3
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maximal stability
647479
7
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unstable
647479
8
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37°C, 15 min, 30% loss of activity
647477
9
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37°C, 15 min, 45% loss of activity
647477
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18
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pH 4.2, t1/2: 5 min
45
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good stability
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the active enzyme is markedly unstable due to rapid autolysis, t1/2: 5 min at 18°C, pH 4.2
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thiol reagent required for stability
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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