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Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
?
benzoyl-Val-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
?
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
?
-
-
?
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
?
-
-
?
benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Gly-Arg + 7-amino-4-methylcoumarin
1% of the activity with Ala-Ala-Phe-7-amido-4-methylcoumarin
-
?
insulin B chain + H2O
?
-
-
?
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Phe + 7-amino-4-methylcoumarin
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
succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
75% of the activity with Ala-Ala-Phe-7-amido-4-methylcoumarin
-
?
tert-butyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
?
tert-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
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
high activity in presence of factor F2
-
?
additional information
?
-
benzoyl-Val-Gly-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Val-Gly-Arg + 7-amino-4-methylcoumarin
5.5% of the activity with Ala-Ala-Phe-7-amido-4-methylcoumarin
-
?
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
benzyloxycarbonyl-Ala-Arg-Arg + 7-amino-4-methylcoumarin
11% of the activity with Ala-Ala-Phe-7-amido-4-methylcoumarin
-
?
benzyloxycarbonyl-Ala-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 7-amino-4-methylcoumarin
high activity in presence of factor F2
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
5.5% of the activity with Ala-Ala-Phe-7-amido-4-methylcoumarin
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
high activity in presence of factor F2
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
1% 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
high activity in presence of factor F2
-
?
additional information
?
-
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
-
?
additional information
?
-
-
structural and mechanistic basis for processive degradation mode of the enzyme, including an electrostatic substrate-to-product sink
-
?
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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
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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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