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Information on EC 3.4.21.B34 - tricorn core protease (archaea)
for references in articles please use BRENDA:EC3.4.21.B34
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preliminary BRENDA-supplied EC number
EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.21 Serine endopeptidases
3.4.21.B34 tricorn core protease (archaea)
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
trilobed protease, tri-scc77, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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CAS REGISTRY NUMBER
COMMENTARY
140879-24-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
Substrates: -
Products: -
Products: -
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
benzoyl-Val-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
Substrates: -
Products: -
Products: -
?
benzoyl-Val-Gly-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Val-Gly-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Ala-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Ala-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Gly-Arg + 7-amino-4-methylcoumarin
Substrates: 1% of the activity with Ala-Ala-Phe-7-amido-4-methylcoumarin
Products: -
Products: -
?
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Phe + 7-amino-4-methylcoumarin
Substrates: 22% of the activity with Ala-Ala-Phe-7-amido-4-methylcoumarin
Products: -
Products: -
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
Substrates: 75% of the activity with Ala-Ala-Phe-7-amido-4-methylcoumarin
Products: -
Products: -
?
tert-butyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
?
Substrates: -
Products: -
Products: -
?
tert-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
Substrates: 2% of the activity with Ala-Ala-Phe-7-amido-4-methylcoumarin
Products: -
Products: -
?
tert-butyloxycarbonyl-Leu-Leu-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Leu-Leu-Arg + 7-amino-4-methylcoumarin
Substrates: high activity in presence of factor F2
Products: -
Products: -
?
benzoyl-Val-Gly-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Val-Gly-Arg + 7-amino-4-methylcoumarin
Substrates: 5.5% of the activity with Ala-Ala-Phe-7-amido-4-methylcoumarin
Products: -
Products: -
?
benzoyl-Val-Gly-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Val-Gly-Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Ala-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 7-amino-4-methylcoumarin
Substrates: 11% of the activity with Ala-Ala-Phe-7-amido-4-methylcoumarin
Products: -
Products: -
?
benzyloxycarbonyl-Ala-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 7-amino-4-methylcoumarin
Substrates: high activity in presence of factor F2
Products: -
Products: -
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
Substrates: 5.5% of the activity with Ala-Ala-Phe-7-amido-4-methylcoumarin
Products: -
Products: -
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
Substrates: high activity in presence of factor F2
Products: -
Products: -
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
Substrates: 1% of the activity with Ala-Ala-Phe-7-amido-4-methylcoumarin
Products: -
Products: -
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
Substrates: high activity in presence of factor F2
Products: -
Products: -
?
additional information
?
-
Substrates: no cleavage of succinyl-Leu-Tyr-7-amido-4-methylcoumarin, succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin, succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin and benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin
Products: -
Products: -
?
additional information
?
-
-
Substrates: structural and mechanistic basis for processive degradation mode of the enzyme, including an electrostatic substrate-to-product sink
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Asp-Gln-Thr-Gln-Lys-Gln-Tyr-Gln-Glu-Leu-Thr-Phe-Phe-chloromethyl ketone
-
carbobenzoxy-L-Leu-L-Leu-L-leucinal
i.e. MG-132, 0.2 mM, 64% inhibition
tosyl-L-phenylalanine-chloromethylketone
0.2 mM, 90% inhibition
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TRI_THEAC
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
1071
0
121623
Swiss-Prot
-
TRI_THEVO
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
1030
0
116998
Swiss-Prot
-
TRI1_STRCO
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
1067
0
115647
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
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
hexamer
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
hexamer
in vivo the hexamers assemble further to form large icosahedral capsids of 14.6 MDa
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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
-
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, 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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tamura, N.; Pfeifer, G.; Baumeister, W.; Tamura, T.
Tricorn protease in bacteria: characterization of the enzyme from Streptomyces coelicolor
Biol. Chem.
382
449-458
2001
Streptomyces coelicolor (Q9RDE2), Streptomyces coelicolor
brenda
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
brenda
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)
brenda
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)
brenda
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)
brenda
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)
brenda
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)
brenda
Kawashima, T.; Amano, N.; Koike, H.; Makino, S.I.; Higuchi, S.; Kawashima-Ohya, Y.; Watanabe, K.; yamazaki, M.; Kanehori, K.; Kawamoto, T.; Nunoshiba, T.; Yamamoto, Y.; Aramaki, H.; makino, K.; Suzuki, M.
Archaeal adaption to higher temperatures revealed by genomic sequence of Thermoplasma volcanium
Proc. Natl. Acad. Sci. USA
97
14257-14262
2000
Thermoplasma volcanium (Q97A95)
brenda
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)
brenda
Bosch, J.; Tamura, T.; Tamura, N.; Baumeister, W.; Essen, L.O.
The beta-propeller domain of the trilobed protease from Pyrococcus furiosus reveals an open Velcro topology
Acta Crystallogr. Sect. D
D63
179-187
2007
Pyrococcus furiosus
brenda
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