Information on EC 3.4.25.1 - proteasome endopeptidase complex

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.25.1
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RECOMMENDED NAME
GeneOntology No.
proteasome endopeptidase complex
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cleavage of peptide bonds with very broad specificity
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
140879-24-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
cv. Bugang
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Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
hawkmoth
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Manually annotated by BRENDA team
Mus musculus C57BL/6
eight-week-old female mice
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Manually annotated by BRENDA team
tobacco
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
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Manually annotated by BRENDA team
variant Ibiza
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain RutC-30
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Manually annotated by BRENDA team
(subunit alpha 1), A0A075KLC7 (subunit alpha 2), A0A075KQM0 (subunit alpha 3), A0A075KJQ7 (subunit alpha 4), A0A075KKH0 (subunit alpha 5), A0A075KK24 (subunit alpha 6), A0A075KLD1 (subunit alpha 7), A0A075KQM4 (subunit beta 1), A0A075KJR2 (subunit beta 2), A0A075KKH6 (subunit beta 3), A0A075KK26 (subunit beta 4), A0A075KLD6 (subunit beta 5), A0A075KQM7 (subunit beta 6), A0A075KJR6 (subunit beta 7)
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-aminocyclopropane-1-carboxylic acid synthase 6 + H2O
?
show the reaction diagram
-
phosphorylation of 1-aminocyclopropane-1-carboxylic acid synthase 6 introduces negative charges to the C-terminus of ACS6, which reduces the turnover of 1-aminocyclopropane-1-carboxylic acid synthase 6 by the 26S proteasome degradation machinery
-
-
?
4-hydroxy-3-nitrophenol-Leu-Leu-Asn-vinylsulfone + H2O
?
show the reaction diagram
-
-
?
4-hydroxy-3-nitrophenyl-Leu-Leu-Lys-vinylsulfone + H2O
?
show the reaction diagram
-
-
?
AAF-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
highest activity in testicle, kidney and brain
-
?
acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin + H2O
acetyl-Ala-Pro-norleucine-Leu-Leu + 7-amino-4-methylcoumarin
show the reaction diagram
acetyl-DPSD-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
cleaved by the beta1 subunit of the 20S proteasome
-
-
?
acetyl-EPFD-7-amido-4-carbamoylcoumarin + H2O
?
show the reaction diagram
acetyl-GPLD-7-amido-4-methylcoumarin + H2O
acetyl-GPLD + 7-amino-4-methylcoumarin
show the reaction diagram
acetyl-GPLE-7-amido-4-methylcoumarin + H2O
acetyl-GPLE + 7-amino-4-methylcoumarin
show the reaction diagram
acetyl-GPLL-7-amido-4-methylcoumarin + H2O
acetyl-GPLL + 7-amino-4-methylcoumarin
show the reaction diagram
acetyl-HHSL-7-amido-4-carbamoylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
acetyl-norleucine-Arg-norleucine-Arg-7-amido-4-carbamoylcoumarin + H2O
?
show the reaction diagram
acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD + 7-amino-4-methylcoumarin
show the reaction diagram
acetyl-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-YVAD + 7-amino-4-methylcoumarin
show the reaction diagram
acetyl-YWTQ-7-amido-4-carbamoylcoumarin + H2O
?
show the reaction diagram
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
-
-
-
-
?
Ala-Phe-Lys-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-LRR-4-methyl-7-amido-coumarin + H2O
benzoyl-LRR + 4-methyl-7-amino-coumarin
show the reaction diagram
benzoyl-Phe-Val-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
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-
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?
benzoyl-VGR-4-methyl-7-amido-coumarin + H2O
benzoyl-VGR + 4-methyl-7-amino-coumarin
show the reaction diagram
-
trypsin-like proteasome activity
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-
?
benzoyl-VGR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
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?
benzyl-Val-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
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?
benzyloxycarbonyl-Ala-Ala-Leu-4-nitroanilide + H2O
?
show the reaction diagram
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?
benzyloxycarbonyl-Ala-Arg-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
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?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
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?
benzyloxycarbonyl-ARR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
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?
benzyloxycarbonyl-D-Ala-Leu-Arg-4-nitroanilide + H2O
?
show the reaction diagram
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?
benzyloxycarbonyl-dALR-4-aminobenzoate + H2O
?
show the reaction diagram
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?
benzyloxycarbonyl-FR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
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?
benzyloxycarbonyl-GAPLG-p-aminobenzoate + H2O
?
show the reaction diagram
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-
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?
benzyloxycarbonyl-GGF-p-aminobenzoate + H2O
?
show the reaction diagram
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?
benzyloxycarbonyl-GGL-2-naphthylamide + H2O
?
show the reaction diagram
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?
benzyloxycarbonyl-GGL-4-nitroanilide + H2O
?
show the reaction diagram
-
chymotrypsin-like activity
-
?
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
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?
benzyloxycarbonyl-GGR-2-naphthylamide + H2O
?
show the reaction diagram
-
trypsin-like activity
-
?
benzyloxycarbonyl-GGR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
benzyloxycarbonyl-Gly-Gly-Arg-beta-naphthylamide + H2O
?
show the reaction diagram
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?
benzyloxycarbonyl-Gly-Gly-Leu-4-nitroanilide + H2O
?
show the reaction diagram
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-
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?
benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
benzyloxycarbonyl-Gly-Gly-Leu-p-nitroanilide + H2O
?
show the reaction diagram
benzyloxycarbonyl-Gly-Pro-Ala-Gly-Gly-p-aminobenzoate + aminopeptidase-N + H2O
?
show the reaction diagram
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?
benzyloxycarbonyl-Gly-Pro-Ala-Leu-Ala-p-aminobenzoate + aminopeptidase-N + H2O
?
show the reaction diagram
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?
benzyloxycarbonyl-GPAFG-p-aminobenzoate + H2O
?
show the reaction diagram
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?
benzyloxycarbonyl-GPAGG-4-aminobenzoate + H2O
?
show the reaction diagram
-
highest activity in soleus and brain
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?
benzyloxycarbonyl-GPAGG-4-nitroanilide + H2O
?
show the reaction diagram
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?
benzyloxycarbonyl-GPALG-4-aminobenzoate + H2O
?
show the reaction diagram
benzyloxycarbonyl-GPALG-p-aminobenzoate + H2O
?
show the reaction diagram
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?
benzyloxycarbonyl-LAF-4-aminobenzoate + H2O
?
show the reaction diagram
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?
benzyloxycarbonyl-Leu-Leu-Glu-2-naphthylamide + H2O
?
show the reaction diagram
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?
benzyloxycarbonyl-Leu-Leu-Glu-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
11% of the activity with succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
?
benzyloxycarbonyl-Leu-Leu-Glu-beta-naphthylamide + H2O
?
show the reaction diagram
benzyloxycarbonyl-Leu-Leu-Leu-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
36% of the activity with succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
?
benzyloxycarbonyl-LLE-2-naphthylamide + H2O
?
show the reaction diagram
benzyloxycarbonyl-LLE-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-LLE-beta-naphthylamide + H2O
?
show the reaction diagram
-
caspase-like activity
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-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-RR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
beta-casein + H2O
?
show the reaction diagram
-
-
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?
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
Boc-Leu-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
Boc-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin + H2O
Boc-Leu-Ser-Thr-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
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?
Bz-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Bz-DL-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
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?
Bz-VGR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
DBC2 protein + H2O
?
show the reaction diagram
-
-
-
-
?
dihydrofolate reductase + H2O
?
show the reaction diagram
ERM transcription factor + H2O
?
show the reaction diagram
-
-
-
-
?
erythroid Krueppel-like factor + H2O
?
show the reaction diagram
-
-
-
-
?
fructose-1,6-bisphosphatase + H2O
?
show the reaction diagram
-
-
-
-
?
Glu-Gly-Gly-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
H-VLK-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
very-low activity
-
?
hepatitis B virus X protein + H2O
?
show the reaction diagram
-
-
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?
IGF-1 + H2O
?
show the reaction diagram
-
-
-
-
?
IkappaBalpha + H2O
?
show the reaction diagram
-
can be directly degraded by 20S proteasomes. Deletion constructs of IkappaBalpha allow us to the determine that N-terminal (DELTA1-70)and C-terminal regions (DELTA280-327, removing the PEST region) of IkappaBalpha are not required for IkappaBalpha degradation,while a further C-terminal deletion including part of the arm repeats (DELTAC2 245-327) almost completely suppress the degradation by 20S proteasome. Degradation of IkappaBalpha involves specific interactions with a C3 subunit of the proteasome
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-
?
Ile-Ile-Trp-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-Arg-Arg + H2O
?
show the reaction diagram
-
-
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-
?
Leu-Leu-Glu + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-Leu-Val-Tyr + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
MATalpha2 repressor + H2O
?
show the reaction diagram
-
-
-
-
?
methyl-casein + H2O
?
show the reaction diagram
-
-
-
-
?
N-Cbz-Leu-Leu-Glu-beta-naphthylamide + H2O
?
show the reaction diagram
-
-
-
-
?
N-methoxysuccinyl-Glu-Val-Lys-Met-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
show the reaction diagram
N-succinyl-LLVY-aminoluciferin + H2O
?
show the reaction diagram
-
-
-
-
?
N-t-Boc-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
N-tert-butyloxycarbonyl-LSTR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
highest activity in kidney
-
?
ovalbumin + H2O
?
show the reaction diagram
-
-
-
-
?
oxidized insulin B chain + H2O
?
show the reaction diagram
-
-
-
-
?
p27(KIP1) + H2O
?
show the reaction diagram
-
-
-
-
?
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
PS1/gamma-secretase complex component + H2O
?
show the reaction diagram
S-RNase + H2O
?
show the reaction diagram
-
S-RNase is ubiquitinated and degraded by the 26S proteasome
-
-
?
Suc-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + Suc-Leu-Leu-Val-Tyr
show the reaction diagram
-
-
-
-
?
Suc-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
succinyl-AAF-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
succinyl-Ile-Ile-Trp-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + 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
succinyl-Leu-Met-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-LLVY-aminoluciferin + H2O
succinyl-LLVY + aminoluciferin
show the reaction diagram
t-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
t-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
tert-butyloxycarbonyl-LRR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
65% of the activity with succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
?
Tyr-Val-Ala-Asp-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
ubiquitinylated proteins
?
show the reaction diagram
unstable green fluorescence protein + H2O
?
show the reaction diagram
-
artificial substrate for the proteasome. The model proteasomal substrate is stabilized by the carboxyl-terminal half of S5a, S5aC
-
-
?
Z-Ala-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Z-Leu-Leu-Glu-7-amido-4-methylcoumarin + H2O
Z-Leu-Leu-Glu + 7-amino-4-methylcoumarin
show the reaction diagram
Z-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
Z-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
Z-LLE-2-naphthylamide + H2O
Z-LLE + 2-naphthylamine
show the reaction diagram
-
post-acidic proteasome activity
-
-
?
Z-LLE-4-methyl-7-amido-coumarin + H2O
Z-LLE + 4-methyl-7-amino-coumarin
show the reaction diagram
Z-LLE-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Z-LRR-aminoluciferin + H2O
?
show the reaction diagram
-
-
-
-
?
Z-nLPnLD-aminoluciferin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
dihydrofolate reductase + H2O
?
show the reaction diagram
-
directly hydrolyzed by the 20S complex, without any previous ubiquitination. The degradation is increased under oxidative conditions. The folate metabolism may be impaired by an increased degradation of dihydrofolate reductase, mediated by the 20S proteasome
-
-
?
PS1/gamma-secretase complex component + H2O
?
show the reaction diagram
-
gamma-secretase components are PS1, nicastrin, Pen-2, and Aph-1. Degradation of the complex components involves the proteasome, but regulation of their activity involves the PI3K/Akt pathway, overview. PS1/gamma-secretase is involved in the activation of phosphatidylinositol-3 kinase/Akt pathway, and is responsible for the intramembranous cleavage of various type-I membrane proteins. PS1/gamma-secretase is also deeply involved in the production of amyloid beta protein
-
-
?
ubiquitinylated proteins
?
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
-
0.3 mM Cd2+ lead to a 1.6 and 2.3fold increase in the 20S proteasome activity after 3 and 10 days, respectively, in leaves, the chymotrypsin activity of the 20S proteasome is maximally increased only after 3 days of treatment with 0.03 mM and 0.3 mM Cd2+ (1.5 and 2.5fold, respectively), no major effect of Cd2+ on the chymotrypsin activity of the 20S proteasome is observed in roots or leaves of plant treated with low Cd2+ concentrations (0.0003 mM and 0.003 mM)
Cl-
-
stimulates chymotrypsin-like activity
Mn2+
-
stimulates chymotrypsin-like activity
Na+
-
100 mM, decreases the rate of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin and succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin 2fold
PMSF
-
activates chymotrypsin-like activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(-)-epigallocatechin-3-gallate
-
i.e. EGCG, inhibits the proteasomal chymotrypsin-like activity
(2E)-3-(4-tert-butylphenyl)-1-[4-(4-nitrophenyl)piperazin-1-yl]prop-2-en-1-one
-
-
(2R,3S)-1,2,3,4-tetrahydronaphthalene-2,3-diyl bis(3,4,5-triethoxybenzoate)
-
inhibits 48% of MDA-MB-231 cell proliferation at 0.05 mM
(2R,3S)-1,2,3,4-tetrahydronaphthalene-2,3-diyl bis(3,4,5-trihydroxybenzoate)
-
-
(2R,3S)-1,2,3,4-tetrahydronaphthalene-2,3-diyl bis(3,5-diethoxybenzoate)
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70-79% inhibition in MDA-MB-231 cells at 0.025-0.050 mM
(2R,3S)-1,2,3,4-tetrahydronaphthalene-2,3-diyl bis(3,5-dihydroxybenzoate)
-
-
(acetato-kappaO)[2,4-diiodo-6-({[(pyridin-2-yl-kappaN)methyl]amino-kappaN}methyl)phenolato-kappaO]copper
-
a copper complex, causes selective 20S proteasomal inhibition and apoptosis induction in several lines of cancer cells
1-[1-(1-[(2,4-dioxoimidazolidin-1-ylimino)-methyl]-2-phenyl-ethylcarbamoyl)-2-(1H-indol-3-yl)-ethylcarbamoyl]-2-(1H-indol)
2-(2-bromo-4-tert-butylphenoxy)-1-[4-(4-nitrophenyl)piperazin-1-yl]ethanone
-
-
2-(2-chlorophenyl)-N-[4-(1,3-thiazol-2-ylsulfamoyl)phenyl]quinoline-4-carboxamide
-
-
2-(4-tert-butylphenoxy)-1-[4-(4-methoxy-2-nitrophenyl)piperazin-1-yl]ethanone
-
-
2-methyl-5-[4-(phenylamino)phthalazin-1-yl]-N-(tetrahydrofuran-2-ylmethyl)benzenesulfonamide
-
-
3,4-dichloroisocoumarin
4-(4-methoxyphenyl)-N-(4-nitrophenyl)piperazine-1-carbothioamide
-
-
4-hydroxy-2-nonenal
-
specific subunits of the 20S proteasome are targeted for modification by 4-hydroxy-2-nonenal (0.5 mM)
4-tert-butyl-N-[4-(diethylsulfamoyl)phenyl]benzamide
-
-
4-tert-butyl-N-[4-(dipropylsulfamoyl)phenyl]benzamide
-
-
4-tert-butyl-N-[4-[di(prop-2-en-1-yl)sulfamoyl]phenyl]benzamide
-
-
acetyl-Ala-Pro-norleucine-Leu-Asp-aldehyde
acetyl-DPSD-CHO
-
-
acetyl-Leu-Leu-Arg
-
IC50: 0.85 mM for chymotrypsin-like activity, 0.0056 mM for trypsin-like activity
acetyl-Leu-Leu-norleucinal
-
competitive
AEBSF
-
25% inhibition of hydrolysis of acetyl-norleucine-Leu-Pro-norleucine-Leu-Asp-7-amino-4-methylcoumarin, 22% inhibition of hydrolysis of acetyl-norleucine-GPLD-7-amido-4-methylcoumarin, 19% inhibition of hydrolysis of acetyl-GPLL-7-amido-4-methylcoumarin, 21% inhibition of hydrolysis of acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin, 26% inhibition of hydrolysis of succinyl-LLVY-7-amido-4-methylcoumarin, 98% inhibition of hydrolysis of tert-butyloxycarbonyl-LRR-7-amino-4-methylcoumarin
ALLN
-
-
antipain
Aprotinin
-
0.0133 mg/ml, 53.62% inhibition
ATP
-
inhibits trypsin-like, peptidylglutamyl peptide hydrolase, and branched-chain amino acid preferring activities
belactosin A
-
isolated from a Streptomyces sp. strain
Belactosin C
-
isolated from a Streptomyces sp. strain
benzyloxycarbonyl-Ala-Ala-Phe-CH2Cl
-
-
benzyloxycarbonyl-GPAF aldehyde
-
-
benzyloxycarbonyl-GPFL aldehyde
-
-
benzyloxycarbonyl-IE-(Ot-Bu)-AL aldehyde
-
0.002 mg/ml, 75% inhibition of chymotrypsin-like activity, hydrolysis of benzyloxycarbonyl-GGL-4-nitroanilide. 0.002 mM, 8% inhibition of peptidyl-glutamyl-peptide-hydrolyzing activity, hydrolysis of benzyloxycarbonyl-LLE-2-naphthylamide
benzyloxycarbonyl-Leu-Gly-Arg
-
IC50: 0.11 mM for chymotrypsin-like activity, 0.0066 mM for trypsin-like activity
benzyloxycarbonyl-Leu-Leu
-
0.1 mM, 84% inhibition of hydrolysis of succinyl-Leu-leu-Val-Tyr-7-amido-4-methylcoumarin, 43% inhibition of hydrolysis of tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin, 20% inhibition of hydrolysis of benzyloxycarbonyl-Leu-Leu-Leu-7-amido-4-methylcoumarin, 86% inhibition of hydrolysis of benzyloxycarbonyl-Leu-Leu-Glu-7-amido-4-methylcoumarin
Benzyloxycarbonyl-Leu-Leu-Arg
-
IC50: 0.056 mM for chymotrypsin-like activity, 0.0014 mM for trypsin-like activity
benzyloxycarbonyl-Leu-Leu-CH2Cl
-
-
benzyloxycarbonyl-Leu-Leu-Leu-CHO
-
reversible inhibitor, modulation by sodium ion
benzyloxycarbonyl-Leu-Ser-Arg
-
IC50: 0.017 mM for chymotrypsin-like activity, 0.0017 mM for trypsin-like activity
benzyloxycarbonyl-Leu-Thr-Arg
-
IC50: 0.065 mM for chymotrypsin-like activity, 0.0021 mM for trypsin-like activity
benzyloxycarbonyl-LLF aldehyde
-
-
benzyloxycarbonyl-LLL aldehyde
-
0.001 mg/ml, 69% inhibition of chymotrypsin-like activity, hydrolysis of benzyloxycarbonyl-GGL-4-nitroanilide
benzyloxycarbonyl-Phe-Ser-Arg
-
IC50: 0.0089 mM for chymotrypsin-like activity, 0.002 mM for trypsin-like activity
-
benzyloxycarbonyl-Pro-norleucine-Leu-Asp-aldehyde
bortezomib
Calpeptin
-
inhibits calpain-like activity
carbobenzoxy-L-leucyl-L-leucyl-leucinal
-
MG-132
carfilzomib
CEP-18770
Cetyltrimethylammonium bromide
-
-
chloro[2,4-diiodo-6-({[(pyridin-2-yl-kappaN)methyl]amino-kappaN}methyl)phenolato-kappaO]copper
-
a copper complex, causes selective 20S proteasomal inhibition and apoptosis induction in several lines of cancer cells
chymostatin
Cl-
-
inhibits peptidylglutamyl peptide hydrolase activity
clasto-lactacystin beta-lactone
-
complete inhibition of the chymotrypsin-like activity at 0.01 mM, complete inhibition of the trypsin-like activity at 0.02 mM, and complete inhibition of caspase-activity of the 26S proteasome at 0.02 mM
clastolactacystin-beta-lactone
-
-
Cystatin
-
0.0133 mg/mL 46.38% inhibition
-
c[Ala-Leu-Leu-Glu(Leu-vinyl ester)]
-
-
c[Gly-Leu-Leu-Glu(Leu-vinyl ester)]
-
-
c[Ser-Leu-Leu-Glu(Leu-vinyl ester)]
-
-
c[Val-Leu-Leu-Glu(Leu-vinyl ester)]
-
-
dibromo[(dimethylamino)methanedithiolato(2-)-kappa2S1,S1]aurate(3-)
-
proteasome inhibition and apoptosis induction are completely blocked by addition of dithiothreitol or N-acetyl-L-cysteine, showing that process of oxidation is required for proteasome inhibition
diisopropylfluorophosphate
-
-
E-64
-
0.0133 mg/ml, 71.15% inhibition
E-64-d
-
0.1 mM, 30% inhibition of hydrolysis of succinyl-Leu-leu-Val-Tyr-7-amido-4-methylcoumarin, no inhibition of hydrolysis of tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin, benzyloxycarbonyl-Leu-Leu-Leu-7-amido-4-methylcoumarin, benzyloxycarbonyl-Leu-Leu-Glu-7-amido-4-methylcoumarin
epoxomicin
epoxomycin
ethanol
-
ethanol-induced proteasome inhibition in liver cells
glial fibrillary acidic protein
-
human recombinant GFP-tagged, accumulation of the intermediate filament protein, glial fibrillary acidic protein, GFAP, in astrocytes of Alexander disease impairs proteasome function in astrocytes, also oligomers of R239C mutant GFAP inhibit the proteasome system in Alexander disease astrocytes to an even higher extent compared to the wild-type GFAP. The small heat shock protein chaperone alphaB-crystallin reverses the inhibition by shifting the size of the mutant protein from larger oligomers to smaller oligomers and monomers. The proteasome cannot efficiently degrade unassembled R239C GFAP, and the interaction of R239C GFAP with proteasomes actually inhibits proteasomal protease activity in a non-competitive manner, detailed overview
-
glidobactin A
-
GlbA
H-Ala-Leu-Leu-Glu(Leu-vinyl ester)-NH2
-
-
H-Gly-Leu-Leu-Glu(Leu-vinyl ester)-NH2
-
-
H-Ser-Leu-Leu-Glu(Leu-vinyl ester)-NH2
-
-
H-Val-Leu-Leu-Glu(Leu-vinyl ester)-NH2
-
-
hepatitis B virus X protein
-
-
-
Histone H3
-
activity with benzyloxycarbonyl-LAF-4-aminobenzoate, 87%, benzyloxycarbonyl-dALR-4-aminobenzoate, 43%, or benzyloxycarbonyl-LLE-2-naphthylamide, 81% as substrates
-
iodoacetic acid
-
1.0 mM, 54.04 mM inhibition
lactacystin
Leupeptin
marizomib
-
-
-
MG-132
MLN9708
Mn2+
-
inhibits peptidylglutamyl peptide hydrolase activity
mutant huntingtin
-
mutant huntingtin filamentous aggregates can inhibit 26S proteasome activity, but only when not recruited inclusion bodies
-
N,N'-bis(4-methoxyphenyl)tricyclo[3.3.1.13,7]decane-1,3-dicarboxamide
-
-
N-(1-hydroxy-2-methylpropan-2-yl)-5-[4-[(3-hydroxyphenyl)amino]phthalazin-1-yl]-2-methylbenzenesulfonamide
-
-
N-(3-hydroxy-2-oxopropyl)-5-[4-[(3-hydroxyphenyl)amino]phthalazin-1-yl]-2-methylbenzenesulfonamide
-
-
N-(4-methoxyphenyl)-3-(4-methylphenyl)tricyclo[3.3.1.13,7]decane-1-carboxamide
-
-
N-(tert-butoxycarbonyl)-L-alanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
-
N-(tert-butoxycarbonyl)-L-alanyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
-
-
N-(tert-butoxycarbonyl)-L-isoleucyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
-
N-(tert-butoxycarbonyl)-L-phenylalanyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
-
60.06% inhibition at 0.01 mM
N-(tert-butoxycarbonyl)-L-phenylalanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
-
N-(tert-butoxycarbonyl)-O-methyl-L-tyrosyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-tyrosinamide
-
89.7% inhibition at 0.01 mM
N-(tert-butoxycarbonyl)-O-methyl-L-tyrosyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
-
69.7% inhibition at 0.01 mM
N-(tert-butoxycarbonyl)glycyl-N1-benzyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-L-glutamamide
-
shows significant inhibition of 20S proteasome chymotrypsin-like, b5 activity
N-(tert-butoxycarbonyl)glycyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
shows significant inhibition of 20S proteasome chymotrypsin-like, b5 activity
N-(tert-butoxycarbonyl)glycyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
-
-
N-acetyl-Leu-Leu-norleucinal
-
-
N-acetyl-leucyl-leucyl-norleucinal
-
MG132, 0.03 mM
N-carbobenzoxy-L-leucyl-L-norvalinal
-
-
N-Cbz-Leu-Leu-leucinal
-
MG132
N-ethylmaleimide
N-methoxysuccinyl-Glu-Val-Lys-Phe-H
-
modified
N-tert-butyl-5-[4-[(3-hydroxyphenyl)amino]phthalazin-1-yl]-2-methylbenzenesulfonamide
-
-
N-tosylphenylalanylchloromethylketone
-
-
N-[(1S)-1-benzyl-2-[[(1S)-1-(furan-2-ylcarbonyl)-3-methylbutyl]amino]-2-oxoethyl]-Na-(tert-butoxycarbonyl)-L-phenylalaninamide
-
inhibits chymotrypsin-like activity of the 26S proteasome
N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-phenylalaninamide
-
58.5% inhibition at 0.01 mM
N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
-
73.4% inhibition at 0.01 mM
N-[(benzyloxy)carbonyl]-L-phenylalanyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
-
82.2% inhibition at 0.01 mM
N-[4-(acetylsulfamoyl)phenyl]-2-(4-ethoxyphenyl)quinoline-4-carboxamide
-
-
N-[4-(acetylsulfamoyl)phenyl]-2-(4-ethylphenyl)quinoline-4-carboxamide
-
-
N-[4-(azepan-1-ylsulfonyl)phenyl]-4-tert-butylbenzamide
-
-
N-[4-(benzylsulfamoyl)phenyl]-2-methylbenzamide
-
-
N-[4-(benzylsulfamoyl)phenyl]-2-[4-(thiophen-2-yl)phenyl]quinoline-4-carboxamide
-
-
N2-(decylcarbamoyl)-N-[(3E,5S,8S,9E)-2,7-dioxo-5-(propan-2-yl)-1,6-diazacyclododeca-3,9-dien-8-yl]-L-valinamide
-
rational design and synthesis of a syringolin A-based lipophilic derivative, which proves to be a very potent syrbactin-based proteasome inhibitor
N2-(tert-butoxycarbonyl)-N-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-3-[(naphthalen-2-ylmethyl)amino]-3-oxo-D-alaninamide
-
-
N2-(tert-butoxycarbonyl)-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
-
N2-(tert-butoxycarbonyl)-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
-
-
Nalpha-(tert-butoxycarbonyl)-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-phenylalaninamide
-
7.7% inhibition at 0.01 mM
Nalpha-(tert-butoxycarbonyl)-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-tyrosinamide
-
16.5% inhibition at 0.01 mM
Nalpha-(tert-butoxycarbonyl)-N-[(2S)-1-[[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]-O-methyl-L-tyrosinamide
-
73% inhibition at 0.01 mM
Nalpha-[(2S)-2-[2-(tert-butoxycarbonyl)hydrazinyl]-4-phenylbutanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-phenylalaninamide
-
-
Nalpha-[(2S)-2-[[(benzyloxy)carbonyl]amino]-4-(4-methoxyphenyl)butanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-tyrosinamide
-
84.8% inhibition at 0.01 mM
Nalpha-[(2S)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-phenylalaninamide
-
47.5% inhibition at 0.01 mM
Nalpha-[(2S)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-tyrosinamide
-
67.1% inhibition at 0.01 mM
Nalpha-[(2S)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
-
14.9% inhibition at 0.01 mM
Nalpha-[(benzyloxy)carbonyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-phenylalaninamide
-
5.7% inhibition at 0.01 mM
Nalpha-[(benzyloxy)carbonyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-tyrosinamide
-
13.6% inhibition at 0.01 mM
Nalpha-[(benzyloxy)carbonyl]-N-[(2S)-1-[[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]amino]-3-(4-methoxyphenyl)-1-oxopropan-2-yl]-O-methyl-L-tyrosinamide
-
60.5% inhibition at 0.01 mM
Nalpha-[(benzyloxy)carbonyl]-N-[(2S)-1-[[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
-
36.4% inhibition at 0.01 mM
NH4+
-
-
NH4Cl
-
lysosomal inhibitor
NLVS
-
irreversible inhibitor
NMDA
-
exposure causes the disassembly of 26S proteasomes and dissociation of E3, i.e. KCMF1, HUWE1, and UBE3A
NPI-0052
NPLLLVS
IC50: 0.04 mM, inhibition of hydrolysis of Gly-Gly-Arg-7-amido-4-methylcoumarin. IC50: 0.007 mM, inhibition of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin, most potent inhibitor for hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
NPLLNVS
IC50: 0.063 mM, inhibition of hydrolysis of Gly-Gly-Arg-7-amido-4-carbamoylcoumarin. IC50: 0.077 mM, inhibition of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
ONX0912
-
a selective, irreversible inhibitor of the chymotrypsin-like activity of constitutive proteasome 20S and immunoproteasome 20S. ONX0912 exerts toxicity in Waldenstroem macroglobulinemia cells, by reducing bone marrow-derived interleukin-6 and insulin-like growth factor 1 secretion, thus inhibiting BM-induced p-Akt and phosphorylated extracellular signal-related kinase activation in Waldenstroem macroglobulinemia cells, overview. ONX0912 acts synergistically with bortezomib
p-chloromercuribenzoic acid
p65/relA
-
inhibits the degradation of IkappaBalpha by the proteasome
-
PA28
-
inhibition of the protease activities of the of the 20S- and 26S proteasome in all larvaeal stages, overview
-
Pentamidine
-
-
Pepstatin
-
0.0133 mg/ml 76.09% inhibition
phenylmethylsulfonyl fluoride
PI 1
-
0.03 mM
prion protein
-
recombinant mouse aggregated beta-PrP binds directly to human 20S and 26S proteasomes, i.e. its 20S core particle, overview. Conversion of cellular prion protein, PrPC, to toxic beta-sheet isoforms, PrPSc, which inhibit the ubiquitin-proteasome system and lead to accumulation of the system substrates, are associated with the prion diseases. PrP aggregates inhibit by stabilising the closed conformation of the substrate entry channel. The 20S proteasome is not inhibited when the gate in the alpha-ring is open due to a truncation mutation or by association with PA26/PA28. Modelling of location of aggregated beta-sheet rich PrP binding to the 20S proteasome and inhibition mechanism, detailed overview
-
pro-epigallocatechin-3-gallate
-
i.e. pro-EGCG, inhibitory efficacy is greatly improved from 42% inhibition to 89% inhibition when combined with 3,5-dinitrocatechol
PS-341
PSI
-
0.1 mM, 93% inhibition of hydrolysis of succinyl-Leu-leu-Val-Tyr-7-amido-4-methylcoumarin, no inhibition of hydrolysis of tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin and benzyloxycarbonyl-Leu-Leu-Leu-7-amido-4-methylcoumarin, complete inhibition of hydrolysis of benzyloxycarbonyl-Leu-Leu-Glu-7-amido-4-methylcoumarin
quercetin
-
-
syringolin A
syringolin A methyl ester
-
-
-
syringolin B
-
SylB, synthesis and inhibitory potency, overview
TLCK
-
0.133 mg/ml, 79.57% inhibition
YLLLVS
IC50: 0.048 mM, inhibition of hydrolysis of Gly-Gly-Arg-7-amido-4-methylcoumarin. IC50: 0.033 mM, inhibition of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
YU102
-
89% inhibition of hydrolysis of acetyl-norleucine-Leu-Pro-norleucine-Leu-Asp-7-amido-4-methylcoumarin, 89% inhibition of hydrolysis of acetyl-norleucine-GPLD-7-amido-4-methylcoumarin, 85% inhibition of hydrolysis of acetyl-GPLL-7-amino-4-methylcoumarin, 84% inhibition of hydrolysis of acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin, 29% inhibition of hydrolysis of succinyl-LLVY-7-amido-4-methylcoumarin, no inhibition of hydrolysis of tert-butyloxycarbonyl-LRR-7-amido-4-methylcoumarin
-
Z-b-Ala-Val-Ser-Leu-vinyl ester
-
-
Z-beta-Ala-Leu-Leu-Leu-vinyl ester
-
-
Z-Gly-Leu-Leu-Leu-vinyl ester
-
-
Z-Gly-Val-Ser-Leu-vinyl ester
-
-
Z-NH-(CH2)3-CO-Leu-Leu-Leu-vinyl ester
-
-
Z-NH-(CH2)3-CO-Val-Ser-Leu-vinyl ester
-
-
Z-NH-(CH2)4-CO-Leu-Leu-Leu-vinyl ester
-
-
Z-NH-(CH2)4-CO-Val-Ser-Leu-vinyl ester
-
-
Z-NH-(CH2)5-CO-Leu-Leu-Leu-vinyl ester
-
-
Z-NH-(CH2)5-CO-Val-Ser-Leu-vinyl ester
-
-
Z-NH-(CH2)6-CO-Leu-Leu-Leu-vinyl ester
-
-
Z-NH-(CH2)6-CO-Val-Ser-Leu-vinyl ester
-
-
Z-NH-(CH2)7-CO-Leu-Leu-Leu-vinyl ester
-
-
Z-NH-(CH2)7-CO-Val-Ser-Leu-vinyl ester
-
-
Zn2+
-
inhibits peptidylglutamyl peptide hydrolase activity
[Au(ESDT)]2
[AuBr2(ESDT)]
[Cu(HLI)(LI)]OAc
-
a copper complex, HLI is the ligand 2,4-diiodo-6-((pyridine-2-ylmethylamino)methyl)phenol, causes selective 20S proteasomal inhibition and apoptosis induction in several lines of cancer cells
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19S regulatory complex
-
represents the major proteasome activator
-
19S regulatory particle
-
-
-
3H-1,2-dithiole-3-thione
-
tissue specific increase of the catalytic subunits of the proteasome following oral administration of 0.5 mmol/kg
aflatoxin G1
-
specific stimulator of activity
Blm10 protein
-
-
-
chymostatin
-
0.05 mg/ml, activation to 170% of the original activity, peptidyl-glutamyl-peptide-hydrolyzing activity, hydrolysis of benzyloxycarbonyl-LLE-2-naphthylamide
doxorubicin
-
apoptosis inductor doxorubicin increases enzymatic activities, regulates subunit composition, and phosphorylation state of 26S proteasomes
Histone H3
-
slective activation of the branched-chain amino acid preferring activity with benzyloxycarbonyl-GPALG-4-aminobenzoate as substrate, 1000%
-
Leupeptin
-
0.05 mg/ml, activation to 125% of the original activity, peptidyl-glutamyl-peptide-hydrolyzing activity, hydrolysis of benzyloxycarbonyl-LLE-2-naphthylamide
nuclear factor erythroid-derived 2-related factor 1
PA28
-
protein activator
-
poly-L-lysine
-
stimulates chymotrypsin-, trypsin- and Staphylococcus aureus V8-like activities
polylysine
-
stimulates caseinolytic activity
protein kinase A
-
protein kinase A treatment drastically enhances 20S peptidase activities in a dose-dependent fashion
-
Rpt2
-
the 19S ATPase subunits, Rpt2 and Rpt5, bind ATP, their C-termini dock into intersubunit pockets in the 20S particle alpha-ring and induce gate opening, activating the protease activity. A conserved HbYX motif in the C-terminus is required
-
Rpt5
-
the 19S ATPase subunits, Rpt2 and Rpt5, bind ATP, their C-termini dock into intersubunit pockets in the 20S particle alpha-ring and induce gate opening, activating the protease activity. A conserved HbYX motif in the C-terminus is required
-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.032 - 0.088
acetyl-EPFD-7-amido-4-carbamoylcoumarin
0.36
acetyl-HHSL-7-amido-4-carbamoylcoumarin
-
pH 7.5, 25C
0.11 - 0.67
acetyl-norleucine-Arg-norleucine-Arg-7-amido-4-carbamoylcoumarin
0.027 - 0.038
acetyl-YWTQ-7-amido-4-carbamoylcoumarin
0.1
benzoyl-VGR-7-amido-4-methylcoumarin
-
-
0.248
benzyloxycarbonyl-ARR-7-amido-4-methylcoumarin
-
-
2.29
benzyloxycarbonyl-GGF-4-aminobenzoate
-
enzyme from thymus
0.751
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin
-
-
0.798
benzyloxycarbonyl-GGR-7-amido-4-methylcoumarin
-
-
0.38 - 3.3
benzyloxycarbonyl-GPAFG-4-aminobenzoate
0.14 - 0.57
benzyloxycarbonyl-GPALG-4-aminobenzoate
0.048
benzyloxycarbonyl-Leu-Leu-Leu-7-amido-4-methylcoumarin
-
-
0.255
benzyloxycarbonyl-LLE-2-naphthylamide
-
-
0.12
benzyloxycarbonyl-LLE-7-amido-4-methylcoumarin
-
-
0.051
benzyloxycarbonyl-RR-7-amido-4-methylcoumarin
-
-
0.01054
beta-casein
-
at 37C
-
0.07
N-succinyl-LLVY 7-amido-4-methylcoumarin
-
-
1.504
succinyl-AAF-7-amido-4-methylcoumarin
-
-
0.089
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
-
0.263
succinyl-LLVY-7-amido-4-methylcoumarin
-
-
0.2
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.97 - 2.7
acetyl-EPFD-7-amido-4-carbamoylcoumarin
36.3
acetyl-HHSL-7-amido-4-carbamoylcoumarin
Homo sapiens
-
pH 7.5, 25C
0.031 - 8.15
acetyl-norleucine-Arg-norleucine-Arg-7-amido-4-carbamoylcoumarin
0.27 - 4.67
acetyl-YWTQ-7-amido-4-carbamoylcoumarin
2.94
benzyloxycarbonyl-ARR-7-amido-4-methylcoumarin
Struthio camelus
-
-
0.2
benzyloxycarbonyl-GGF-4-aminobenzoate
Bos taurus
-
enzyme from thymus
16.9
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin
Struthio camelus
-
-
0.052 - 2.1
benzyloxycarbonyl-GGR-7-amido-4-methylcoumarin
Struthio camelus
-
-
1.98 - 18.8
benzyloxycarbonyl-GPAFG-4-aminobenzoate
0.03 - 12.9
benzyloxycarbonyl-GPALG-4-aminobenzoate
0.332
benzyloxycarbonyl-LLE-2-naphthylamide
Struthio camelus
-
-
0.143
benzyloxycarbonyl-RR-7-amido-4-methylcoumarin
Struthio camelus
-
-
6.08
succinyl-LLVY-7-amido-4-methylcoumarin
Struthio camelus
-
-
additional information
succinyl-AAF-7-amido-4-methylcoumarin
Struthio camelus
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
acetyl-Ala-Pro-norleucine-Leu-Asp-aldehyde
-
-
0.002 - 0.0026
benzyloxycarbonyl-GPAF aldehyde
0.00005 - 0.0527
benzyloxycarbonyl-GPFL aldehyde
0.0016 - 0.00597
benzyloxycarbonyl-LLF aldehyde
0.021
benzyloxycarbonyl-Pro-norleucine-Leu-Asp-aldehyde
-
-
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000086 - 0.000194
(-)-epigallocatechin-3-gallate
Homo sapiens
-
inhibition of the chymotrypsin-like activity of the proteasome in vitro, pH not specified in the publication, temperature not specified in the publication
0.019
(2R,3S)-1,2,3,4-tetrahydronaphthalene-2,3-diyl bis(3,4,5-trihydroxybenzoate)
Homo sapiens
-
for the chymotrypsin-like activity, pH 7.5, 37C
0.029
(2R,3S)-1,2,3,4-tetrahydronaphthalene-2,3-diyl bis(3,5-dihydroxybenzoate)
Homo sapiens
-
for the chymotrypsin-like activity, pH 7.5, 37C
0.00022
1-[1-(1-[(2,4-dioxoimidazolidin-1-ylimino)-methyl]-2-phenyl-ethylcarbamoyl)-2-(1H-indol-3-yl)-ethylcarbamoyl]-2-(1H-indol)
Homo sapiens
-
pH 7.5, 30C
0.85
acetyl-Leu-Leu-Arg
Patiria pectinifera
-
IC50: 0.85 mM for chymotrypsin-like activity, 0.0056 mM for trypsin-like activity
0.11
benzyloxycarbonyl-Leu-Gly-Arg
Patiria pectinifera
-
IC50: 0.11 mM for chymotrypsin-like activity, 0.0066 mM for trypsin-like activity
0.056
Benzyloxycarbonyl-Leu-Leu-Arg
Patiria pectinifera
-
IC50: 0.056 mM for chymotrypsin-like activity, 0.0014 mM for trypsin-like activity
0.017
benzyloxycarbonyl-Leu-Ser-Arg
Patiria pectinifera
-
IC50: 0.017 mM for chymotrypsin-like activity, 0.0017 mM for trypsin-like activity
0.065
benzyloxycarbonyl-Leu-Thr-Arg
Patiria pectinifera
-
IC50: 0.065 mM for chymotrypsin-like activity, 0.0021 mM for trypsin-like activity
0.0089
benzyloxycarbonyl-Phe-Ser-Arg
Patiria pectinifera
-
IC50: 0.0089 mM for chymotrypsin-like activity, 0.002 mM for trypsin-like activity
-
0.0074
dibromo[(dimethylamino)methanedithiolato(2-)-kappa2S1,S1]aurate(3-)
Oryctolagus cuniculus
-
inhibition of the chymotrypsin-like activity of the 20S proteasome
0.000049 - 0.002
glidobactin A
0.0347
KAuBr4
Oryctolagus cuniculus
-
-
0.1
Leupeptin
Trypanosoma brucei
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
IC50: 0.0015 mM, inhibition of hydrolysis of Gly-Gly-Arg-7-amido-4-methylcoumarin, most potent inhibitor for hydrolysis of Gly-Gly-Arg-7-amido-4-methylcoumarin. IC50: 0.1 mM, inhibition of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
0.0000373
MG-132
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37C
0.00084 - 0.01
N-(tert-butoxycarbonyl)-L-alanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
0.00428 - 0.01
N-(tert-butoxycarbonyl)-L-alanyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
0.0015 - 0.01
N-(tert-butoxycarbonyl)-L-isoleucyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
0.00942
N-(tert-butoxycarbonyl)-L-phenylalanyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37C
0.00147 - 0.01
N-(tert-butoxycarbonyl)-L-phenylalanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
0.00164
N-(tert-butoxycarbonyl)-O-methyl-L-tyrosyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-tyrosinamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37C
0.00815
N-(tert-butoxycarbonyl)-O-methyl-L-tyrosyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37C
0.00054 - 0.01
N-(tert-butoxycarbonyl)glycyl-N1-benzyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-L-glutamamide
0.00028 - 0.01
N-(tert-butoxycarbonyl)glycyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
0.00274 - 0.01
N-(tert-butoxycarbonyl)glycyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
0.00785
N-[(1S)-1-benzyl-2-[[(1S)-1-(furan-2-ylcarbonyl)-3-methylbutyl]amino]-2-oxoethyl]-Na-(tert-butoxycarbonyl)-L-phenylalaninamide
Homo sapiens
-
-
0.00756
N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-phenylalaninamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37C
0.00585
N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37C
0.00262
N-[(benzyloxy)carbonyl]-L-phenylalanyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37C
0.00000865 - 0.0000796
N2-(decylcarbamoyl)-N-[(3E,5S,8S,9E)-2,7-dioxo-5-(propan-2-yl)-1,6-diazacyclododeca-3,9-dien-8-yl]-L-valinamide
0.00451 - 0.01
N2-(tert-butoxycarbonyl)-N-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-3-[(naphthalen-2-ylmethyl)amino]-3-oxo-D-alaninamide
0.00723 - 0.01
N2-(tert-butoxycarbonyl)-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
0.00068 - 0.01
N2-(tert-butoxycarbonyl)-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
0.01
Nalpha-(tert-butoxycarbonyl)-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-phenylalaninamide
0.00682
Nalpha-(tert-butoxycarbonyl)-N-[(2S)-1-[[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]-O-methyl-L-tyrosinamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37C
0.00785
Nalpha-[(2S)-2-[2-(tert-butoxycarbonyl)hydrazinyl]-4-phenylbutanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-phenylalaninamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37C
0.00327
Nalpha-[(2S)-2-[[(benzyloxy)carbonyl]amino]-4-(4-methoxyphenyl)butanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-tyrosinamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37C
0.00839
Nalpha-[(2S)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-phenylalaninamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37C
0.00642
Nalpha-[(2S)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-tyrosinamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37C
0.01
Nalpha-[(2S)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
0.00601
Nalpha-[(benzyloxy)carbonyl]-N-[(2S)-1-[[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]amino]-3-(4-methoxyphenyl)-1-oxopropan-2-yl]-O-methyl-L-tyrosinamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37C
0.01
Nalpha-[(benzyloxy)carbonyl]-N-[(2S)-1-[[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
Homo sapiens
-
IC50 above 0.01 mM, in 10 mM HEPES (pH 7.6), at 37C
0.007
NPLLLVS
Trypanosoma brucei
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
IC50: 0.04 mM, inhibition of hydrolysis of Gly-Gly-Arg-7-amido-4-methylcoumarin. IC50: 0.007 mM, inhibition of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin, most potent inhibitor for hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-meth
0.077
NPLLNVS
Trypanosoma brucei
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
IC50: 0.063 mM, inhibition of hydrolysis of Gly-Gly-Arg-7-amido-4-carbamoylcoumarin. IC50: 0.077 mM, inhibition of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
0.00102 - 0.0103
syringolin A
0.000757 - 0.0187
syringolin A methyl ester
0.00778 - 0.1078
syringolin B
0.033
YLLLVS
Trypanosoma brucei
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
IC50: 0.048 mM, inhibition of hydrolysis of Gly-Gly-Arg-7-amido-4-methylcoumarin. IC50: 0.033 mM, inhibition of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
additional information
additional information
Homo sapiens
-
cell growth inhibition activities, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0013
-
substrate succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin
0.0077
-
-
0.0091
-
substrate carbobenzoxy-Leu-Leu-Glu-beta-naphthylamide
0.016
-
-
3.47
-
-