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Information on EC 3.4.21.B34 - tricorn core protease (archaea) and Organism(s) Thermoplasma acidophilum and UniProt Accession P96086

for references in articles please use BRENDA:EC3.4.21.B34
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.B34 tricorn core protease (archaea)
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This record set is specific for:
Thermoplasma acidophilum
UNIPROT: P96086
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The taxonomic range for the selected organisms is: Thermoplasma acidophilum
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
trilobed protease, tri-scc77, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY hide
140879-24-9
-
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
-
-
?
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
high activity in presence of factor F2
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
high activity in presence of factor F2
-
?
benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
?
insulin B chain + H2O
?
show the reaction diagram
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
high activity in presence of factor F2
-
?
tert-butyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
?
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
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Asp-Gln-Thr-Gln-Lys-Gln-Tyr-Gln-Glu-Leu-Thr-Phe-Phe-chloromethyl ketone
-
benzyloxycarbonyl-Phe-PSI[CO-CONH]Arg-Glu-Phe-OH
-
decanoyl-Arg-Val-Arg-Lys-chloromethyl ketone
-
tosyl-L-phenylalanine chloromethyl ketone
-
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
calculation from nucleotide sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
720000
gel filtration
SUBUNIT
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
hanging drop vapour diffusion method
-
hanging drop vapour diffusion method, crystal structure at 2.0 resolution, recombinant protein
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
PROTEIN VARIANTS
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
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brandstetter, H.; Kim, J.S.; Groll, M.; Gottig, P.; Huber, R.
Structural basis for the processive protein degradation by tricorn protease
Biol. Chem.
383
1157-1165
2002
Thermoplasma acidophilum
Manually annotated by BRENDA team
Tamura, N.; Lottspeich, F.; Baumeister, W.; Tamura, T.
The role of tricorn protease and its aminopeptidase-interacting factors in cellular protein degradation
Cell
95
637-648
1998
Thermoplasma acidophilum (P96086)
Manually annotated by BRENDA team
Ponting, C.P.; Pallen, M.J.
beta-Propeller repeats and a PDZ domain in the tricorn protease: predicted self-compartmentalisation and C-terminal polypeptide-binding strategies of substrate selection
FEMS Microbiol. Lett.
179
447-451
1999
Thermoplasma acidophilum (P96086)
Manually annotated by BRENDA team
Kim, J.S.; Groll, M.; Musiol, H.J.; Behrendt, R.; Kaiser, M.; Moroder, L.; Huber, R.; Brandstetter, H.
Navigation inside a protease: substrate selection and product exit in the tricorn protease from Thermoplasma acidophilum
J. Mol. Biol.
324
1041-1050
2002
Thermoplasma acidophilum (P96086)
Manually annotated by BRENDA team
Bosch, J.; Tamura, T.; Bourenkov, G.; Baumeister, W.; Essen, L.O.
Purification, crystallization, and preliminary X-ray diffraction analysis of the Tricorn protease hexamer from Thermoplasma acidophilum
J. Struct. Biol.
134
83-87
2001
Thermoplasma acidophilum (P96086)
Manually annotated by BRENDA team
Brandstetter, H.; Kim, J.S.; Groll, M.; Huber, R.
Crystal structure of the tricorn protease reveals a protein disassembly line
Nature
414
466-470
2001
Thermoplasma acidophilum (P96086)
Manually annotated by BRENDA team
Tamura, T.; Tamura, N.; Cejka, Z.; Hegerl, R.; Lottspeich, F.; Baumeister, W.
Tricorn protease--the core of a modular proteolytic system
Science
274
1385-1389
1996
Thermoplasma acidophilum (P96086)
Manually annotated by BRENDA team