Information on EC 3.4.21.B34 - tricorn core protease (archaea)

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
3.4.21.B34
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
tricorn core protease (archaea)
-
CAS REGISTRY NUMBER
COMMENTARY hide
140879-24-9
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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 + H2O
?
show the reaction diagram
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
benzoyl-Val-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
benzoyl-Val-Gly-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Val-Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
benzyloxycarbonyl-Ala-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
1% of the activity with Ala-Ala-Phe-7-amido-4-methylcoumarin
-
?
casein + H2O
?
show the reaction diagram
-
-
-
?
insulin B chain + H2O
?
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
22% of the activity with Ala-Ala-Phe-7-amido-4-methylcoumarin
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
75% of the activity with Ala-Ala-Phe-7-amido-4-methylcoumarin
-
?
tert-butyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
tert-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
2% of the activity with Ala-Ala-Phe-7-amido-4-methylcoumarin
-
?
tert-butyloxycarbonyl-Leu-Leu-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Leu-Leu-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
high activity in presence of factor F2
-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
100 mM KCl, enhances activity to 121% of control
Mg2+
25 mM MgCl2, 7fold enhancement of peptidase activity
Mn2+
25 mM MnCl2, enhances activity to 141% of the control
Na+
100 mM NaCl, enhances activity to 132% of control
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ala-Ala-Phe-chloromethylketone
500 nM, 90% inhibition
Asp-Gln-Thr-Gln-Lys-Gln-Tyr-Gln-Glu-Leu-Thr-Phe-Phe-chloromethyl ketone
-
-
benzyloxycarbonyl-Phe-PSI[CO-CONH]Arg-Glu-Phe-OH
-
-
Ca2+
100 mM, CaCl2, 57% inhibition
carbobenzoxy-L-Leu-L-Leu-L-leucinal
i.e. MG-132, 0.2 mM, 64% inhibition
decanoyl-Arg-Val-Arg-Lys-chloromethyl ketone
-
-
NEM
1 mM, enzyme retains 87% of its activity
tosyl-L-phenylalanine chloromethyl ketone
-
-
tosyl-L-phenylalanine-chloromethylketone
0.2 mM, 90% inhibition
Zn2+
25 mM ZnCl2, 60% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
factor F2
-
increases activity
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
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calculation from nucleotide sequence
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
117000
6 * 117000, SDS-PAGE
120000
-
6 * 120000, the hexameric toroid can assemble further into a capsid structure. Tricorn protease appears to act as a core of a proteolytic system, when it interacts with several smaller proteins, it displays multicatalytic activities, SDS-PAGE
220000
-
SDS-PAGE
700000
gel filtration
720000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
monomer
-
the domain architecture of the monomeric enzyme is consistent with two beta-propeller structures that act to exclude large folded substrates, a PDT domain that binds substrates‘ C-terminal sequences and a Tsp-like serine protease domain that mediates cleavage site-specific substrate hydrolysis
trimer
-
x-ray crystallography
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, with 100 mM sodium acetate pH 4.4, 20 mM MgCl2, 300 mM 1,6-hexanediol and 10% (w/v) PEG 4000
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enzyme in complex with inhibitor: decanoyl-Arg-Val-Arg-Lys-chloromethyl ketone, Asp-Gln-Thr-Gln-Lys-Gln-Tyr-Gln-Glu-Leu-Thr-Phe-Phe-chloromethyl ketone or benzyloxycarbonyl-Phe-PSI[CO-CONH]Arg-Glu-Phe-OH, hanging drop vapour diffusion method
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hanging drop vapour diffusion method
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hanging drop vapour diffusion method, crystal structure at 2.0 resolution, recombinant protein
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hanging drop vapour diffusion method, forms crystals of octahedral morphology under low-ionic-strength conditions. Crystals belong to space group C2 with unit cell dimensions, a = 307.5 A, b = 163.2 A, c =220.9 A, beta = 105.5° and diffract to 2.2 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)-RIL cells
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expression in Escherichia coli
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expression of Tri-SCC77 in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L184C
-
increase in activity with benzoyl-Val-Gly-Arg-7-amido-4-methylcoumarin and insulin B chain to more than 150% of the wild-type activity, no activity with casein
R131E/R132E
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slight decrease in activity with benzoyl-Val-Gly-Arg-7-amido-4-methylcoumarin, strong decrease in activity with insulin B chain, barely detectable activity with casein
R414C/A643C
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decrease in activity with benzoyl-Val-Gly-Arg-7-amido-4-methylcoumarin to 70% of wild-type activity, decrease in activity with insulin B chain as substrate to 50% of wild-type activity, no activity with casein