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
3.4.25.1
-
RECOMMENDED NAME
GeneOntology No.
proteasome endopeptidase complex
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cleavage of peptide bonds with very broad specificity
show the reaction diagram
mechanism
-
cleavage of peptide bonds with very broad specificity
show the reaction diagram
chymotrypsin-like activity and peptidylglutamyl peptide hydrolase activity
-
cleavage of peptide bonds with very broad specificity
show the reaction diagram
ATPase activity
-
cleavage of peptide bonds with very broad specificity
show the reaction diagram
Staphylococcus aureus V8 protease like activity
-
cleavage of peptide bonds with very broad specificity
show the reaction diagram
peptidylglutamyl peptide hydrolase, chymotrypsin-like and trypsin-like activities
-
cleavage of peptide bonds with very broad specificity
show the reaction diagram
chymotrypsin-like activity
-
cleavage of peptide bonds with very broad specificity
show the reaction diagram
chymotrypsin-like, trypsin-like and V8 protease like activities
-
cleavage of peptide bonds with very broad specificity
show the reaction diagram
trypsin-like, chymotrypsin-like activities, peptidylglutamyl peptide hydrolase and branched-chain amino acid preferring and caseinolytic activities
-
cleavage of peptide bonds with very broad specificity
show the reaction diagram
ATPase activity, chymotrypsin-like activity, trypsin-like activity
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 S proteasome
-
-
20S proteasome
-
-
20S proteasome
-
-
20S proteasome
Q8I7N8
-
20S proteasome
-
-
20S proteasome
-
-
20S proteasome
-
-
20S proteasome
-
-
20S proteasome
-
-
20S proteasome
-
-
20S proteasome
Q9GU37
-
26S protease
-
-
-
-
26S proteasome
-
-
26S proteasome
-
-
26S proteasome
-
-
26S proteasome
Q9V3P6
-
26S proteasome
-
the 26S proteasome is a large multisubunit complex containing a 20S proteolytic core particle and a 19S regulatory particle
26S proteasome
-
the 26S proteasomes consist of a catalytic 20S core and two 19S regulatory complexes
26S proteasome
-
-
26S proteasome
-
-
26S proteasome
-
-
26S proteasome
-
-
26S proteasome
-
-
26S proteasome complex
-
-
27 kDa prosomal protein
-
-
-
-
30 kDa prosomal protein
-
-
-
-
beta1-PF1404
-
-
c20S
-
-
Component Y8
-
-
-
-
constitutive proteasome 20S
-
-
EC 3.4.99.46
-
-
formerly
-
GPRO-28
-
-
-
-
HsBPROS26
-
-
-
-
HSN3
-
-
-
-
i20S
-
-
immunoproteasome 20S
-
-
ingensin
-
-
-
-
KIPase
-
-
large multicatalytic protease
-
-
-
-
macropain
-
-
-
-
multi-subunit protease complex
-
-
multicatalytic endopeptidase complex
-
-
-
-
Multicatalytic endopeptidase complex C7
-
-
-
-
multicatalytic protease
-
-
-
-
multicatalytic proteinase
-
-
-
-
p27K
-
-
-
-
PROS-27
-
-
-
-
PROS-30
-
-
-
-
PROS-Dm25
-
-
-
-
PROS-Dm28.1
-
-
-
-
PROS-Dm29
-
-
-
-
PROS-Dm35
-
-
-
-
Pros26.4
-
member of the AAA-ATPase subunits of the proteasome 19S regulatory particle
prosome
-
-
-
-
proteasome
-
-
-
-
proteasome
-
-
proteasome 19S
-
-
proteasome 20S
-
-
Proteasome component C13
-
-
-
-
Proteasome component C2
-
-
-
-
Proteasome component C3
-
-
-
-
Proteasome component C5
-
-
-
-
Proteasome component C8
-
-
-
-
Proteasome component C9
-
-
-
-
Proteasome component DD4
-
-
-
-
Proteasome component DD5
-
-
-
-
Proteasome component pts1
-
-
-
-
PSMA5
Q8I7N8
alpha5 subunit of the 20S proteasome
RING12 protein
-
-
-
-
RN3
-
-
-
-
SCL1 suppressor protein
-
-
-
-
TAS-F22/FAFP98
-
-
-
-
TAS-G64
-
-
-
-
TCPR29
-
-
-
-
tricorn protease
-
-
-
-
tricorn proteinase
-
-
-
-
XC3
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
140879-24-9
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Arabidopsis thaliana Col-0
-
-
-
Manually annotated by BRENDA team
cv. Bugang
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
subunit p110
SwissProt
Manually annotated by BRENDA team
subunit p30
UniProt
Manually annotated by BRENDA team
subunit p37A
UniProt
Manually annotated by BRENDA team
subunit p37B
UniProt
Manually annotated by BRENDA team
subunit p39A
UniProt
Manually annotated by BRENDA team
subunit p39B
SwissProt
Manually annotated by BRENDA team
subunit p42A
SwissProt
Manually annotated by BRENDA team
subunit p42B; subunit p48B
-
-
Manually annotated by BRENDA team
subunit p42C
SwissProt
Manually annotated by BRENDA team
subunit p42D
SwissProt
Manually annotated by BRENDA team
subunit p48A
SwissProt
Manually annotated by BRENDA team
subunit p50
SwissProt
Manually annotated by BRENDA team
subunit p54
SwissProt
Manually annotated by BRENDA team
subunit p55
SwissProt
Manually annotated by BRENDA team
subunit P56
SwissProt
Manually annotated by BRENDA team
subunit P58
SwissProt
Manually annotated by BRENDA team
subunit p97
SwissProt
Manually annotated by BRENDA team
expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
hawkmoth
-
-
Manually annotated by BRENDA team
Balb/c mice
-
-
Manually annotated by BRENDA team
C57BL/6 mice
-
-
Manually annotated by BRENDA team
eight-week-old female mice
-
-
Manually annotated by BRENDA team
female CB17-SCID mice
-
-
Manually annotated by BRENDA team
ICR mice
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6
eight-week-old female mice
-
-
Manually annotated by BRENDA team
male sprague-dawley rats
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
Wistar rats
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
variant Ibiza
-
-
Manually annotated by BRENDA team
ostrich
-
-
Manually annotated by BRENDA team
strain RutC-30
-
-
Manually annotated by BRENDA team
alpha1 subunit
SwissProt
Manually annotated by BRENDA team
alpha2 subunit
SwissProt
Manually annotated by BRENDA team
alpha3 subunit
SwissProt
Manually annotated by BRENDA team
alpha4 subunit
SwissProt
Manually annotated by BRENDA team
alpha5 subunit
SwissProt
Manually annotated by BRENDA team
alpha6 subunit
SwissProt
Manually annotated by BRENDA team
alpha7 subunit
SwissProt
Manually annotated by BRENDA team
beta1 subunit
SwissProt
Manually annotated by BRENDA team
beta2 subunit
SwissProt
Manually annotated by BRENDA team
beta3 subunit
SwissProt
Manually annotated by BRENDA team
beta4 subunit
SwissProt
Manually annotated by BRENDA team
beta5 subunit
SwissProt
Manually annotated by BRENDA team
beta6 subunit
SwissProt
Manually annotated by BRENDA team
beta7 subunit
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
reduced proteasomal activity contributes to the accumulation of carbonylated proteins in chronic experimental autoimmune encephalomyelitis. Chymotrysin-like and caspase-like activities of the 20S proteasome are impaired in chronic experimental autoimmune encephalomyelitis, while the amount of proteasome is unchanged, determination of proteasome failure by the build-up of ubiquitinated proteins, mostly within astrocytes, diminished activity of the 20S proteasome is a major contributor to the accumulation of carbonylated proteins in astrocytes of chronic experimental autoimmune encephalomyelitis mice
malfunction
Mus musculus C57BL/6
-
reduced proteasomal activity contributes to the accumulation of carbonylated proteins in chronic experimental autoimmune encephalomyelitis. Chymotrysin-like and caspase-like activities of the 20S proteasome are impaired in chronic experimental autoimmune encephalomyelitis, while the amount of proteasome is unchanged, determination of proteasome failure by the build-up of ubiquitinated proteins, mostly within astrocytes, diminished activity of the 20S proteasome is a major contributor to the accumulation of carbonylated proteins in astrocytes of chronic experimental autoimmune encephalomyelitis mice
-
metabolism
-
inhibition of the proteolytic activity of the proteasome induces apoptosis and suppresses essential functions of activated human CD4+ T cells, and proteasome inhibition activates the mitochondrial pathway of apoptosis in human CD4+ T cells, detailed mechanisms of apoptosis, overview
metabolism
-
the expression of unstable proteins is regulated by transcriptional regulation and not by degradation of the unstable protein by the ubiquitin/proteasome system, overview
physiological function
-
it is possible to restore significant levels of enzyme activity to 17 of 18 disease causing missense mutations in human cystathionine beta-synthase expressed in Saccharomyces cerevisiae by exposure to ethanol, proteasome inhibitors, e.g. bortezomib or MG132, or deletion of the Hsp26 small heat shock protein. All three of these treatments induce Hsp70, which is necessary but not sufficient for rescue, overview. The treatment can also rescue disease-causing mutations in human p53 and the methylene tetrahydrofolate reductase gene
physiological function
-
oxidative stress caused by tert-butyl hydroperoxide and proteasome inhibition by lactacystin induce apoptosis in neurons and astrocytes. Suppression of proteasome activity triggers the translocation of cathepsin D from lysosomes to cytosol, mechanism, overview
physiological function
-
physiological effects of partial inhibition of proteolytic activities of the proteasome, overview
physiological function
-
proteasome inhibition increases the sensitivity of tumor cells toward cytolytic T-cell attack by NOXA-mediated enhancement of mitochondrial second mitochondria-derived activator of caspase, SMAC, release, overview
physiological function
-
the 20S proteasome is a multicatalytic protease playing a crucial role in cellular protein turnover in eukaryotes. It is involved in the maintenance of the biological homeostasis and degradation of key components of the cellmachinery. Critical cellular functions such as transcription, cell-cycle progression, cell differenciation, antigen processing, and tumor suppression rely on this molecular system
physiological function
-
the proteasome, a multicatalytic protease, is responsible for the generation of most MHC class I ligands
physiological function
-
the ubiquitin-proteasome pathway is essential for promoting the exchange of transcriptional factors on chromatin
physiological function
-
the ubiquitin-proteasome system is involved in many cellular functions by mediating selective protein degradation. Protein substrates are first selected and marked by polyubiquitination, polyubiquitinated proteins are next recognized and degraded by the 26S proteasome, which consists of a 20S catalytic core particle and a 19S regulatory particle. Once polyubiquitin on a substrate protein is recruited to the 19S RP, the protein moiety is unfolded, translocated into the 20S CP, and finally degraded with release of polyubiquitin, which is processed into free ubiquitin and recycled
physiological function
-
proteasome-mediated proteolysis is important for synaptic plasticity, neuronal development, protein quality control, and many other processes in neurons. The standard 26S subunits and a set of 28 proteasome-interacting proteins that associate substoichiometrically and may serve as regulators or cofactors in the brain differing in composition from other tissues. The content of proteasomes and their set of associated proteins can be altered by neuronal activity, in a manner likely to influence synaptic plasticity and learning
physiological function
-
the 20S proteasome, which is the major proteolytic enzyme of the cell, is responsible for the generation of antigenic peptides derived from endogenously expressed foreign or aberrant protein molecules. The proteasome-generated spliced peptides are presented by MHC class I molecules to the outside world so that they can be specifically recognised by cytotoxic T lymphocytes at the cell surface. Peptide splicing is an intrinsic additional catalytic property of the proteasome
physiological function
-
the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable
physiological function
-
the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable. Immunoproteasome is responsible for breaking down foreign proteins into short antigenic peptides, which are ligands of MHC class I molecules. ATPase induced gate opening in the 20S CP
physiological function
Rattus norvegicus Sprague-Dawley
-
proteasome-mediated proteolysis is important for synaptic plasticity, neuronal development, protein quality control, and many other processes in neurons. The standard 26S subunits and a set of 28 proteasome-interacting proteins that associate substoichiometrically and may serve as regulators or cofactors in the brain differing in composition from other tissues. The content of proteasomes and their set of associated proteins can be altered by neuronal activity, in a manner likely to influence synaptic plasticity and learning
-
metabolism
-
the ubiquitin-proteasome pathway plays an important role in a variety of cellular functions, primarily via its proteolytic activity, and is one of the vital pathways in the cell that becomes dysfunctional as a result of chronic ethanol consumption. The inhibition of proteasome activity in the nucleus is therefore etiologically involved in the accumulation of damaged proteins in the nucleus, and in the deregulation of transcription
additional information
-
a decrease in proteasome activity induced by the injection of lactacystin in the corpus callosum in the remyelination process that normally occurs after cuprizone-induced demyelination markedly improves the remyelination process. It also attenuates the activation of NFkappaB and the recruitment of microglia and astrocytes, thus helping in the recovery of the mitochondrial respiratory chain activities that are affected by cuprizone treatment
additional information
-
inhibition of the proteasomes by gold complexes results in accumulation of ubiquitinated proteins and proteasome target proteins, and induction of cell death, but at significantly different levels
additional information
-
inhibition of this enzymatic activity with beta-subunit-specific proteasome inhibitors may provide an anti-tumoral effect by inhibiting cell proliferation and angiogenesis, and by selectively inducing apoptosis of tumor cells
additional information
-
primary Waldenstroem macroglobulinemia cells express higher level of immunoproteasome 20S compared with constitutive proteasome 20S. Selective inhibition of the chymotrypsin-like activity of constitutive proteasome 20S and immunoproteasome 20S represents a sufficient and successful strategy to induce antineoplastic effect in hematologic tumors
additional information
-
proteasome inhibitors, but not a Nedd8 pathway inhibitor, upregulate RNA levels of PSM genes in cancer cells
additional information
-
the 26S proteasome consists of a 20S multicatalytic core capped on either end with 19S regulatory subunits. The 20S proteasome is a chambered, barrel-like structure containing two heptameric rings made from alpha subunits and two heptameric rings made from beta subunits. The alpha rings perform capping and gating functions, whereas three of the beta subunits, beta1, beta2, and beta5, contain the NH2-terminal threonines responsible for the different proteasome proteolytic activities. The beta1, beta2, and beta5 subunits are referred to as caspase-like, trypsin-like, and chymotrypsin-like, respectively
additional information
-
the barrel-shaped proteolytic 20S proteasome core particle which consists of four seven-subunit rings, is capped at one or both ends by 19S regulatory particles and is the central part of the large, 2.4 MDa, multi-subunit protease complexes performing ATP-dependent degradation of poly-ubiquitinated proteins, and being responsible for the majority of the non-lysosomal proteolysis which occurs in eukaryotic cells
additional information
-
the proteasomal chymotrypsin-like activity inhibition is associated with accumulated levels of ubiquitinated proteins
additional information
-
activity and subunit composition of the 26 S proteasomes in plants, detailed overview. The 26 S proteasome is composed of two subparticles, the 20 S core protease that compartmentalizes the protease active sites and the 19 S regulatory particle that recognizes and translocates appropriate substrates into the core protease lumen for breakdown. A diverse and highly dynamic population of proteasomes is assembled in plants, which may expand the target specificity and functions of intracellular proteolysis, overview
additional information
-
development of an integrated proteomic approach, QTAX, for quantitative analysis of tandem affinity purified in vivo cross-linked protein complexes to capture protein interactions of all natures in a single analysis, overview. Investigation of cell cycle specific proteasome interaction networks
additional information
-
development of SpliceMet: a method that combines combinatorial computations with mass spectrometric analyses of proteasome-generated spliced peptides, for analysis of peptides, presented by MHC class I molecules on the cell surface, in a manner independent of cytotoxic T lymphocytes, kinetics, detailed overview
additional information
-
structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, 20S CP, detailed overview
additional information
Arabidopsis thaliana Col-0
-
activity and subunit composition of the 26 S proteasomes in plants, detailed overview. The 26 S proteasome is composed of two subparticles, the 20 S core protease that compartmentalizes the protease active sites and the 19 S regulatory particle that recognizes and translocates appropriate substrates into the core protease lumen for breakdown. A diverse and highly dynamic population of proteasomes is assembled in plants, which may expand the target specificity and functions of intracellular proteolysis, overview
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
-
-
?
4-hydroxy-3-nitrophenyl-Leu-Leu-Lys-vinylsulfone + H2O
?
show the reaction diagram
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
-
-
?
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-EPFD-7-amido-4-carbamoylcoumarin + H2O
?
show the reaction diagram
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
-
-
?
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-Arg-norleucine-Arg-7-amido-4-carbamoylcoumarin + H2O
?
show the reaction diagram
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
-
-
?
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
-
-
-
?
acetyl-YWTQ-7-amido-4-carbamoylcoumarin + H2O
?
show the reaction diagram
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + 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
?
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
-
trypsin-like proteasome activity
-
-
?
benzoyl-LRR-4-methyl-7-amido-coumarin + H2O
benzoyl-LRR + 4-methyl-7-amino-coumarin
show the reaction diagram
-
trypsin-like proteasome activity with the specific fluorogenic substrate
-
-
?
benzoyl-Phe-Val-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-VGR-4-methyl-7-amido-coumarin + H2O
benzoyl-VGR + 4-methyl-7-amino-coumarin
show the reaction diagram
-
trypsin-like proteasome activity
-
-
?
benzoyl-VGR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
benzyl-Val-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Leu-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Arg-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-ARR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-D-Ala-Leu-Arg-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-dALR-4-aminobenzoate + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-FR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-GAPLG-p-aminobenzoate + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-GGF-p-aminobenzoate + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-GGL-2-naphthylamide + H2O
?
show the reaction diagram
-
-
-
?
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
-
-
-
?
benzyloxycarbonyl-GGR-2-naphthylamide + H2O
?
show the reaction diagram
-
trypsin-like activity
-
?
benzyloxycarbonyl-GGR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-GGR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
tryspin-like activity
-
-
?
benzyloxycarbonyl-Gly-Gly-Arg-beta-naphthylamide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
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-Gly-Leu-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Ala-Gly-Gly-p-aminobenzoate + aminopeptidase-N + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Ala-Leu-Ala-p-aminobenzoate + aminopeptidase-N + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-GPAFG-p-aminobenzoate + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-GPAGG-4-aminobenzoate + H2O
?
show the reaction diagram
-
highest activity in soleus and brain
-
?
benzyloxycarbonyl-GPAGG-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-GPALG-4-aminobenzoate + H2O
?
show the reaction diagram
-
-
-
-
-
benzyloxycarbonyl-GPALG-4-aminobenzoate + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-GPALG-4-aminobenzoate + H2O
?
show the reaction diagram
-
highest activity in testicle, brain and soleus
-
?
benzyloxycarbonyl-GPALG-p-aminobenzoate + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-LAF-4-aminobenzoate + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Glu-2-naphthylamide + H2O
?
show the reaction diagram
-
-
-
-
?
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-Glu-beta-naphthylamide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Glu-beta-naphthylamide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Glu-beta-naphthylamide + H2O
?
show the reaction diagram
-
-
-
-
?
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-2-naphthylamide + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-LLE-2-naphthylamide + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-LLE-2-naphthylamide + H2O
?
show the reaction diagram
-
highest activity in testicle
-
?
benzyloxycarbonyl-LLE-2-naphthylamide + H2O
?
show the reaction diagram
-
peptidyl-glutamyl-peptide-hydrolyzing activity
-
?
benzyloxycarbonyl-LLE-7-amino-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-LLE-beta-naphthylamide + H2O
?
show the reaction diagram
-
caspase-like activity
-
-
?
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
-
-
-
-
?
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
Mus musculus, Mus musculus C57BL/6
-
for trypsin-like activity
-
-
?
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
Boc-Leu-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
trypsin-like activity
-
-
?
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
Boc-Leu-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
Arabidopsis thaliana, Arabidopsis thaliana Col-0
-
trypsin-like activity
-
-
?
Boc-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin + H2O
Boc-Leu-Ser-Thr-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
?
Bz-VGR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
casein + 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
-
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, directly hydrolyzed by the 20S complex, without any previous ubiquitination. The degradation is increased under oxidative conditions
-
-
?
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
-
-
-
-
?
Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
-
-
?
H-VLK-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
very-low activity
-
?
hepatitis B virus X protein + H2O
?
show the reaction diagram
-
-
-
-
?
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
-
-
?
Ile-Ile-Trp-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-Arg-Arg + H2O
?
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
?
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
?
show the reaction diagram
-
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
highest activity in testicle, liver and spleen
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
show the reaction diagram
-
chymotrypsin-like proteasome activity
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
show the reaction diagram
-
chymotrypsin-like proteasome activity
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
show the reaction diagram
-
chymotrypsin-like proteasome activity
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
show the reaction diagram
-
chymotrypsin-like proteasome activity with the specific fluorogenic substrate
-
-
?
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
-
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, gamma-secretase components are PS1, nicastrin, Pen-2, and Aph-1
-
-
?
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
Mus musculus, Mus musculus C57BL/6
-
for chymotrypsin-like activity
-
-
?
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-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Phe-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
?
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
?
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
?
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
?
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
?
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
?
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
?
show the reaction diagram
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
Q8I7N8
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
chymotrypsin-like activity
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
substrate for chymotrypsin-like activity of the 20S proteasome
-
-
?
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-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
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
Rattus norvegicus Sprague-Dawley
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
Arabidopsis thaliana Col-0
-
-
-
-
?
succinyl-Leu-Met-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-LLVY-aminoluciferin + H2O
succinyl-LLVY + aminoluciferin
show the reaction diagram
-
chymotrypsin-like proteasome activity
-
-
?
succinyl-LLVY-aminoluciferin + H2O
succinyl-LLVY + aminoluciferin
show the reaction diagram
-
chymotrypsin-like proteasome activity
-
-
?
succinyl-LLVY-aminoluciferin + H2O
succinyl-LLVY + aminoluciferin
show the reaction diagram
-
chymotrypsin-like proteasome activity
-
-
?
t-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
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
-
-
-
-
?
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-Leu-Leu-Leu-vinylsulfone + H2O
?
show the reaction diagram
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
-
-
?
Tyr-Val-Ala-Asp-7-amido-4-methylcoumarin + H2O
?
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-Glu-7-amido-4-methylcoumarin + H2O
Z-Leu-Leu-Glu + 7-amino-4-methylcoumarin
show the reaction diagram
Mus musculus, Mus musculus C57BL/6
-
for caspase-like activity
-
-
?
Z-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
Z-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
Mus musculus, Mus musculus C57BL/6
-
for calpain-like activity
-
-
?
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
-
peptidylglutamyl peptide hydrolase proteasome activity
-
-
?
Z-LLE-4-methyl-7-amido-coumarin + H2O
Z-LLE + 4-methyl-7-amino-coumarin
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
-
post-acidic proteasome activity
-
-
?
Z-LLE-4-methyl-7-amido-coumarin + H2O
Z-LLE + 4-methyl-7-amino-coumarin
show the reaction diagram
-
post-acidic proteasome activity with the specific fluorogenic substrate
-
-
?
Z-LLE-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
methyl-casein + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
-
proteasomes are the primary sites for protein degradation in mammalian cells. Each proteasome particle contains two chymotrypsin-like, two trypsin-like, and two caspase-like proteolytic sites. Caspase-like sites cleave after aspartates better than after glutamates
-
?
additional information
?
-
-
the 20S proteasome of Trypanosoma brucei shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
-
proteasomes are the primary sites for protein degradation in mammalian cells. Each proteasome particle contains two chymotrypsin-like, two trypsin-like, and two caspase-like proteolytic sites
-
?
additional information
?
-
-
the chymotrypsin-like and trypsin-like activities, but not the peptidylglutamyl peptide hydrolyzing activity plays a key role in oocyte maturation
-
?
additional information
?
-
-
the tobacco mosaic virus-induced RNP7 subunit may be involved in programmed cell death
-
-
-
additional information
?
-
-
maximal chymotrypsin-like activity of the 20S proteasome, which contributes to the cytolytic mechanism of the natural killer cells, is associated with the conformational changes occuring in a cluster of highly conserved proteasome residues from the alpha-subunit that lead to the proteasome open conformation, allowing substrate access into the proteolytic chamber
-
-
-
additional information
?
-
-
proteasome status in KG1a and U937 cells, overview
-
-
-
additional information
?
-
-
the proteasome is a cylindrical, multicatalytic proteolytic machine with three peptidase activities, chymotryptic, tryptic and postglutamyl peptide hydrolytic
-
-
-
additional information
?
-
-
three major proteolytic activities of the proteasome can be distinguished as trypsin-like, chymotrypsin-like, and peptidyl-glutamyl peptide hydrolase activities, which cleave peptide bonds on the carboxyl side of basic, hydrophobic, and acidic amino acid residues, respectively. The catalytic core of the 20S proteasome is a Thr residue, responsible for the catalytic cleavage of substrates through nucleophilic attack
-
-
-
additional information
?
-
-
proteasome complexes possess three main catalytic activities, which are trypsin-like, chymotrypsin-like, and caspase-like
-
-
-
additional information
?
-
-
substrate docking sites, e.g. S5a, contain ubiquitin-interacting motifs that selectively recruit ubiquinated proteins to the proteasome. Human S5a-ubiquitin-interacting motifs stabilize only a subset of proteasomal substrates. Proliferation of A549 lung cancer cells is inhibited by S5a-ubiquitin-interacting motifs. S5a-ubiquitin-interacting motifs result in an increase in the number of apoptotic G0 cells, presumably because of inhibition of a subset of proteasomal substrate proteins
-
-
-
additional information
?
-
-
the proteasome cannot efficiently degrade unassembled R239C GFAP, and the interaction of R239C GFAP with proteasomes actually inhibits proteasomal protease activity. Soluble wild-type GFAP, but not R239C GFAP, is partially degraded by the 20 S proteasome
-
-
-
additional information
?
-
-
the purified proteasome, comprising 102 distinct proteins, shows high chymotrypsin-like activity, mass spectrometry and protein identifications, overview
-
-
-
additional information
?
-
-
mass spectrometric analysis of proteasome interactions. Several proteasome-interacting proteins unique to synaptic 26S proteasomes, i.e. 14-3-3gamma, TAX1BP1, drebrin, SNAP-25, may modulate proteolysis in a synapse-specific manner. Three E3s, i.e. KCMF1, HUWE1, and UBE3A, and five DUBs, i.e. USP5, USP7, USP13, USP14, and UCH37, in association with synaptic proteasomes, which may help proteasomes function more efficiently, help determine specificity for certain types of conjugates, or insure the rapid elimination of ubiquitin chains released from the substrate
-
-
-
additional information
?
-
-
several other proteins associate with the Arabidopsis thaliana proteasome, including the PBAC2 assembly chaperonin, the associated DSS1/Sem1/RPN15 protein, the deubiquitylating enzyme UBP16, and the alternative activator PA200, genetic analysis of PA200 in Arabidopsis, overview
-
-
-
additional information
?
-
Rattus norvegicus Sprague-Dawley
-
mass spectrometric analysis of proteasome interactions. Several proteasome-interacting proteins unique to synaptic 26S proteasomes, i.e. 14-3-3gamma, TAX1BP1, drebrin, SNAP-25, may modulate proteolysis in a synapse-specific manner. Three E3s, i.e. KCMF1, HUWE1, and UBE3A, and five DUBs, i.e. USP5, USP7, USP13, USP14, and UCH37, in association with synaptic proteasomes, which may help proteasomes function more efficiently, help determine specificity for certain types of conjugates, or insure the rapid elimination of ubiquitin chains released from the substrate
-
-
-
additional information
?
-
Arabidopsis thaliana Col-0
-
several other proteins associate with the Arabidopsis thaliana proteasome, including the PBAC2 assembly chaperonin, the associated DSS1/Sem1/RPN15 protein, the deubiquitylating enzyme UBP16, and the alternative activator PA200, genetic analysis of PA200 in Arabidopsis, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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
-
-
?
additional information
?
-
-
proteasomes are the primary sites for protein degradation in mammalian cells. Each proteasome particle contains two chymotrypsin-like, two trypsin-like, and two caspase-like proteolytic sites
-
?
additional information
?
-
-
the chymotrypsin-like and trypsin-like activities, but not the peptidylglutamyl peptide hydrolyzing activity plays a key role in oocyte maturation
-
?
additional information
?
-
-
the tobacco mosaic virus-induced RNP7 subunit may be involved in programmed cell death
-
-
-
additional information
?
-
-
proteasome status in KG1a and U937 cells, overview
-
-
-
additional information
?
-
-
the proteasome is a cylindrical, multicatalytic proteolytic machine with three peptidase activities, chymotryptic, tryptic and postglutamyl peptide hydrolytic
-
-
-
additional information
?
-
-
three major proteolytic activities of the proteasome can be distinguished as trypsin-like, chymotrypsin-like, and peptidyl-glutamyl peptide hydrolase activities, which cleave peptide bonds on the carboxyl side of basic, hydrophobic, and acidic amino acid residues, respectively. The catalytic core of the 20S proteasome is a Thr residue, responsible for the catalytic cleavage of substrates through nucleophilic attack
-
-
-
additional information
?
-
-
mass spectrometric analysis of proteasome interactions. Several proteasome-interacting proteins unique to synaptic 26S proteasomes, i.e. 14-3-3gamma, TAX1BP1, drebrin, SNAP-25, may modulate proteolysis in a synapse-specific manner. Three E3s, i.e. KCMF1, HUWE1, and UBE3A, and five DUBs, i.e. USP5, USP7, USP13, USP14, and UCH37, in association with synaptic proteasomes, which may help proteasomes function more efficiently, help determine specificity for certain types of conjugates, or insure the rapid elimination of ubiquitin chains released from the substrate
-
-
-
additional information
?
-
-
several other proteins associate with the Arabidopsis thaliana proteasome, including the PBAC2 assembly chaperonin, the associated DSS1/Sem1/RPN15 protein, the deubiquitylating enzyme UBP16, and the alternative activator PA200, genetic analysis of PA200 in Arabidopsis, overview
-
-
-
additional information
?
-
Rattus norvegicus Sprague-Dawley
-
mass spectrometric analysis of proteasome interactions. Several proteasome-interacting proteins unique to synaptic 26S proteasomes, i.e. 14-3-3gamma, TAX1BP1, drebrin, SNAP-25, may modulate proteolysis in a synapse-specific manner. Three E3s, i.e. KCMF1, HUWE1, and UBE3A, and five DUBs, i.e. USP5, USP7, USP13, USP14, and UCH37, in association with synaptic proteasomes, which may help proteasomes function more efficiently, help determine specificity for certain types of conjugates, or insure the rapid elimination of ubiquitin chains released from the substrate
-
-
-
additional information
?
-
Arabidopsis thaliana Col-0
-
several other proteins associate with the Arabidopsis thaliana proteasome, including the PBAC2 assembly chaperonin, the associated DSS1/Sem1/RPN15 protein, the deubiquitylating enzyme UBP16, and the alternative activator PA200, genetic analysis of PA200 in Arabidopsis, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
stimulates the caseinolytic activity
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
stimulates chymotrypsin-like activity
Ca2+
-
stimulates chymotrypsin-like activity
Ca2+
-
stimulates chymotrypsin-like activity
Ca2+
-
significantly stimulates activity of the 20S proteasome at pH 7.5, completely inhibits at pH 5.5
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
K+
-
stimulates chymotrypsin-like activity
K+
-
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
Mg2+
-
stimulates chymotrypsin-like activity
Mg2+
-
stimulates chymotrypsin-like activity
Mg2+
-
stimulates chymotrypsin-like activity
Mg2+
-
significantly stimulates activity of the 20S proteasome at pH 7.5, completely inhibits at pH 5.5
Mg2+
-
enhanced by low concentrations of Mg2+ (5-15 mM)
Mg2+
-
required
Mg2+
-
required
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
Zn2+
-
stimulates chymotrypsin-like activity
Zn2+
-
does not significantly affect the activity of 20S proteasome at pH 7.5, the 20S proteasome expresses lower activity in the presence of Zn2+ ions in solution at the acidic pH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
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)
-
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)
-
-
1-[1-(1-[(2,4-dioxoimidazolidin-1-ylimino)-methyl]-2-phenyl-ethylcarbamoyl)-2-(1H-indol-3-yl)-ethylcarbamoyl]-2-(1H-indol)
-
i.e. S-2209, potently inhibits chymotrypsin-like proteasome activity of the human 20S proteasome. S-2209 targets NFkappaB activity, overview. S-2209 inhibits cell growth and induces apoptosis in human multiple myeloma cells, mechanisms, overview
1-[1-(1-[(2,4-dioxoimidazolidin-1-ylimino)-methyl]-2-phenyl-ethylcarbamoyl)-2-(1H-indol-3-yl)-ethylcarbamoyl]-2-(1H-indol)
-
i.e. S-2209, targets NFkappaB activity, overview
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
-
-
3,4-Dichloroisocoumarin
-
-
3,4-Dichloroisocoumarin
-
-
3,4-Dichloroisocoumarin
-
-
3,4-Dichloroisocoumarin
-
-
3,4-Dichloroisocoumarin
-
benzyloxycarbonyl-GGL-4-nitroanilide as substrate
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
-
99% inhibition of hydrolysis of acetyl-norleucine-Leu-Pro-norleucine-Leu-Asp-7-amido-4-methylcoumarin, complete inhibition of hydrolysis of acetyl-norleucine-GPLD-7-amido-4-methylcoumarin, 95% inhibition of hydrolysis of acetyl-GPLL-7-amido-4-methylcoumarin, 89% inhibition of hydrolysis of acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin, 24% inhibition of hydrolysis of succinyl-LLVY-7-amido-4-methylcoumarin, no inhibition of hydrolysis of tert-butyloxycarbonyl-LRR-7-amino-4-methylcoumarin
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
-
-
antipain
-
0.0133 mg/ml, 74.04% inhibition
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
-
99% inhibition of hydrolysis of acetyl-norleucine-Leu-Pro-norleucine-Leu-Asp-7-amino-4-methylcoumarin, complete inhibition of hydrolysis of acetyl-norleucine-GPLD-7-amido-4-methylcoumarin, 95% inhibition of hydrolysis of acetyl-GPLL-7-amido-4-methylcoumarin, 91% inhibition of hydrolysis of acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin, 12% inhibition of hydrolysis of succinyl-LLVY-7-amido-4-methylcoumarin, no inhibition of hydrolysis of tert-butyloxycarbonyl-LRR-7-amido-4-methylcoumarin
benzyloxycarbonyl-Pro-norleucine-Leu-Asp-aldehyde
-
-
bortezomib
-
also termed VELCADE
bortezomib
-
ONX0912 acts synergistically with bortezomib
bortezomib
-
induces apoptosis in primary myeloma cells, but causes no induction of apoptosis in peripheral blood mononuclear cells from healthy humans
bortezomib
-
the proteasome inhibitor bortezomib sensitizes previously resistant tumor cells, melanoma cells, for cytolytic T-cell attack
bortezomib
-
-
bortezomib
-
an N-terminally blocked Phe-Leu dipeptide inhibitor containing a C-terminal boronic acid, inhibits chymotrypsin-likeand caspase-like actitivities of the proteasome, inhibitory pattern with the chymotrypsin-like activity of the intermediate-proteasome subtypes, overview
bortezomib
-
activates the mitochondrial pathway of apoptosis in activated CD4+ T cells by disrupting the equilibrium of pro-apoptotic and anti-apoptotic proteins at the outer mitochondrial membrane and by inducing the generation of reactive oxygen species
bortezomib
-
proteasome inhibition with bortezomib led to an increased susceptibility to viral infection, e.g. with lymphocytic choriomeningitis virus, and proteasome inhibitors can alter Ag processing in vivo
bortezomib
-
i.e. [(1R)-3-methyl-1-[[(2S)-1-oxo-3-phenyl-2-[(pyrazinylcarbonyl)amino]propyl]amino]butyl]boronic acid, treatment of human respiratory syncytial virus-infected Balb/C mice with the proteasome inhibitor results in increased inflammation and mortality, in contrast to infected Vero cells, overview
Ca2+
-
inhibits peptidylglutamyl peptide hydrolase activity
Ca2+
-
significantly stimulates activity of the 20S proteasome at pH 7.5, completely inhibits at pH 5.5
Ca2+
-
-
Calpeptin
-
inhibits calpain-like activity
carbobenzoxy-L-leucyl-L-leucyl-leucinal
-
MG-132
carfilzomib
-
irreversible
CEP-18770
-
reversible
Cetyltrimethylammonium bromide
-
-
chymostatin
-
inhibits chymotrypsin-like activity
chymostatin
-
partial inhibition
chymostatin
-
-
chymostatin
-
inhibits chymotrypsin-like activity
chymostatin
-
-
chymostatin
-
0.05 mg/ml, 98% inhibition of chymotrypsin-like activity, hydrolysis of benzyloxycarbonyl-GGL-4-nitroanilide. 0.05 mg/ml, 15% inhibition of trypsin-like activity, hydrolysis of benzyloxycarbonyl-GGR-2-naphthylamide
chymostatin
-
0.1 mM, 93% inhibition of hydrolysis of succinyl-Leu-leu-Val-Tyr-7-amido-4-methylcoumarin, 94% inhibition of hydrolysis of tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin, no inhibition of hydrolysis of benzyloxycarbonyl-Leu-Leu-Leu-7-amido-4-methylcoumarin, 93% inhibition of hydrolysis of benzyloxycarbonyl-Leu-Leu-Glu-7-amido-4-methylcoumarin
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
-
-
epoxomicin
-
irreversible inhibitor
epoxomicin
-
inhibits the proteasome and causes cell cycle arrest at G2/M
epoxomicin
-
-
epoxomicin
-
EPOX, a specific proteasome inhibitor, abolishes chymotrypsin-like activity in both wild-type 20S and a3DN 20S mutant proteasomes after pre-treatment with 50 mM epoxomicin
epoxomicin
-
-
epoxomicin
-
inhibition of the protease activities of the of the 20S- and 26S proteasome in all larvaeal stages, overview
epoxomicin
-
inhibits trypsin-like activity
epoxomycin
-
effect on mRNA and protein abundance in HeLa cells, overview
epoxomycin
-
effect on mRNA and protein abundance in NIH-3T3 and N2A cells, overview
epoxomycin
-
effect on mRNA and protein abundance in PC-12 cells, overview
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
K+
-
inhibits peptidylglutamyl peptide hydrolase activity
lactacystin
-
-
lactacystin
-
0.01 mM
lactacystin
-
a specific proteasome inhibitor
lactacystin
-
-
lactacystin
-
specific inhibitor of the proteasome, partial inhibition of proteasome activity enhances remyelination after cuprizone-induced demyelination, overview
lactacystin
-
effect on mRNA and protein abundance in HeLa cells, overview
lactacystin
-
effect on mRNA and protein abundance in NIH-3T3 and N2A cells, overview
lactacystin
-
effect on mRNA and protein abundance in PC-12 cells, overview
lactacystin
-
-
Leupeptin
-
inhibits trypsin-like activity
Leupeptin
-
inhibits trypsin-like activity
Leupeptin
-
inhibits trypsin-like activity
Leupeptin
-
inhibits trypsin-like activity
Leupeptin
-
inhibits trypsin-like activity
Leupeptin
-
-
Leupeptin
-
0.05 mg/ml, 25% inhibition of chymotrypsin-like activity, hydrolysis of benzyloxycarbonyl-GGL-4-nitroanilide. 0.05 mg/ml, 88% inhibition of trypsin-like activity, hydrolysis of benzyloxycarbonyl-GGR-2-naphthylamide
Leupeptin
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
Leupeptin
-
0.0133 mg/ml, 53.19% inhibition
MG-132
-
reversible inhibitor
MG115
-
0.1 mM, 99% inhibition of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin, 80% inhibition of hydrolysis of tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin, 61% inhibition of hydrolysis of benzyloxycarbonyl-Leu-Leu-Leu-7-amido-4-methylcoumarin, complete inhibition of hydrolysis of benzyloxycarbonyl-Leu-Leu-Glu-7-amido-4-methylcoumarin
MG132
-
0.1 mM, 98% inhibition of hydrolysis of succinyl-Leu-leu-Val-Tyr-7-amido-4-methylcoumarin, 13% inhibition of hydrolysis of tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin, 82% inhibition of hydrolysis of benzyloxycarbonyl-Leu-Leu-Leu-7-amido-4-methylcoumarin, complete inhibition of hydrolysis of benzyloxycarbonyl-Leu-Leu-Glu-7-amido-4-methylcoumarin
MG132
-
0.01 mM
MG132
-
0.001 mM
MG132
-
31% residual chymotrypsin-like activity at 0.04 mM, 24% residual trypsin-like activity at 0.04 mM, and complete inhibition of caspase-activity of the 26S proteasome at 0.02 mM
MG132
-
0.02 mM
MG132
-
0.05 mM
MG132
-
i.e. Z-Leu-Leu-Leu-aldehyde, inhibits the chymotrypsin-like proteasome activity, inhibitory pattern with the chymotrypsin-like activity of the intermediate-proteasome subtypes, overview. Does not affect the caspase-like activity of subtypes II-2, I,-3, and I-4 at all
MG132
-
effect on mRNA and protein abundance in HeLa cells, overview
MG132
-
effect on mRNA and protein abundance in NIH-3T3 and N2A cells, overview
MG132
-
effect on mRNA and protein abundance in PC-12 cells
MG132
-
CP inhibitor
Mg2+
-
inhibits peptidylglutamyl peptide hydrolase activity
Mg2+
-
inhibits trypsin like activity
Mg2+
-
significantly stimulates activity of the 20S proteasome at pH 7.5, completely inhibits at pH 5.5
MLN9708
-
an N-capped dipeptidyl leucine boronic acid, a potent inhibitor of the proteasome in tumor cells
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-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
-
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
-
inhibits trypsin-like and chymotrypsin-like activities
N-ethylmaleimide
-
-
N-ethylmaleimide
-
1.0 mM, 31.91% inhibition
N-methyoxysuccinyl-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-[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
-
-
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
-
irreversible
NPLLLVS
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-methylcoumarin
NPLLNVS
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
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
-
-
p-chloromercuribenzoic acid
-
-
p-chloromercuribenzoic acid
-
0.1 mM, 6.4% inhibition
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
-
inhibits trypsin-like activity
phenylmethylsulfonyl fluoride
-
-
phenylmethylsulfonyl fluoride
-
0.1 mM, 75.36% inhibition
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
-
use in cancer therapy
PS-341
-
reversible inhibitor
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
-
-
SDS
-
inhibits peptidylglutamyl peptide hydrolase activity
SDS
-
inhibits trypsin-like and chymotrypsin-like activities
SDS
-
inhibits trypsin-like activity
SDS
-
trypsin-like activity, hydrolysis of benzyloxycarbonyl-GGR-2-naphthylamide
SDS
-
significantly stimulates activity of the 20S proteasome at pH 7.5, completely inhibits at pH 5.5
syringolin A
-
a tripeptide derivative, from Pseudomonas putida pv. syringae B728a, consisting of an N-terminal valine followed by the two non-proteinogenic amino acids 3,4-dehydrolysine and 5-methyl-4-amino-2-hexenoic acid, the latter two forming a twelve-membered macrolactam ring, irreversibly inhibits the eukaryotic proteasome, mechanism, overview. The biosynthesis of the compound involves genes sylA-sylE, structure, overview
syringolin A
-
SylA, synthesis and inhibitory potency, overview
syringolin A methyl ester
-
-
-
syringolin B
-
SylB, synthesis and inhibitory potency, overview
TLCK
-
0.133 mg/ml, 79.57% inhibition
YLLLVS
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
Yu101
-
-
Yu101
-
Nrf1-/- mouse embryonic fibroblasts are impaired in the recovery of proteasome activity after transient treatment with the covalent proteasome inhibitor YU101
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
-
i.e. AUL15, a gold(I)-dithiocarbamato species, inhibits the chymotrypsin-like activity of purified 20S proteasome and 26S proteasome in breast cancer cells
[Au(ESDT)]2
-
i.e. AUL15, a gold(I)-dithiocarbamato species, inhibits the chymotrypsin-like activity of purified 20S proteasome
[AuBr2(ESDT)]
-
i.e. AUL12, a gold(III)-dithiocarbamato species, inhibits the chymotrypsin-like activity of purified 20S proteasome and 26S proteasome in breast cancer cells
[AuBr2(ESDT)]
-
i.e. AUL12, a gold(III)-dithiocarbamato species, inhibits the chymotrypsin-like activity of purified 20S proteasome
[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
-
[Cu(LI)Cl]
-
a copper complex, causes selective 20S proteasomal inhibition and apoptosis induction in several lines of cancer cells
[Cu(LI)OAc]
-
a copper complex, causes selective 20S proteasomal inhibition and apoptosis induction in several lines of cancer cells
Mn2+
-
inhibits peptidylglutamyl peptide hydrolase activity
additional information
-
proteasome inhibition by lipofuscin/ceroid during postmitotic aging of fibroblasts
-
additional information
-
although inhibitors of the caspase-like sites allosterically inhibit the chymotrypsin-like activity, inhibitors of the caspase-like sites allosterically inhibit the chymotrypsin-like activity. When caspase-like sites are occupied by the uncleaved propeptide or inhibitor, their substrates still inhibit the chymotrypsin like activity
-
additional information
-
inhibition of purified 20S proteasome and 26S proteasome activities by epigallocatechin-3-gallate and its analogues, overview
-
additional information
-
design and synthesis of boron peptide analogue proteasome inhibitors based on the structure of belactosin C, overview
-
additional information
-
design and screening method development for protease inhibitors, that do not induce the proteasome, overview
-
additional information
-
no direct inhibition of the proteasome by LY294002, but treatment with phosphatidylinositol-3 kinase inhibitors LY294002 or wortmannin, leads to increased levels of PS1/gamma-secretase components through an inhibitory effect on their degradation. Phosphatidylinositol-3 kinase inhibition may trigger the multiple mono-ubiquitination of PS1, which precludes the degradation of PS1/gamma-secretase through the proteasomal pathway, overview
-
additional information
-
study of potent and selective inhibition of the 20S proteasome beta1 catalytic subsite by a series of vinyl ester cyclopeptide analogues synthesized on the basis of a class of cyclopeptides derived from linear prototype inhibitors, in which the exocyclic pharmacophoric unit Leu-vinyl ester is linked to the c-carboxyl group of the glutamic acid residue at the C-terminus. The compounds inhibit the caspase-like activity of the proteasome at nanomolar concentrations, and demonstrate good resistance to proteolysis and a capacity to permeate the cell membrane
-
additional information
-
screening of compounds for in vitro capacity to inhibit the chymotryptic-, tryptic-like, and post-acidic activities of the proteasome, overview. Detection of N-terminal-prolonged vinyl ester-based peptides as selective proteasome beta1 subunit inhibitors. The inhibitors demonstrate resistance to plasmatic proteases and a good capacity to permeate the cell membrane, but low inhibitory potencies. Inhibitors of the post-acidic activity of proteasomes neither induce cell death nor greatly inhibit cell proliferation
-
additional information
-
MLN9708 has a shorter proteasome dissociation half-life and improved pharmacokinetics, pharmacodynamics, and antitumor activity compared with bortezomib in clinical trials
-
additional information
-
assignment of species [CuLI]+ as the minimal pharmacophore needed for proteasomal chymotryspin-like activity inhibition, copper complex synthesis and structures, overview. The proteasomal chymotrypsin-like activity is inhibited by 45%, 60%,70% and 80% after 2, 4, 8, and 18 h, respectively, by the copper complexes in C4-2B prostate cancer cells, overview
-
additional information
-
gold(I)- and gold(III)-compound-mediated proteasome inhibition and cell death induction are completely reversed by the addition of reducing agents, e.g. dithiothreitol or N-acetyl-L-cysteine
-
additional information
-
detection of drug-like proteasome inhibitrs by a multistep structure-based virtual ligand screening strategy, effects on trypsin-like, chymotrypsin-like, and post-acidic proteasome activities, overview
-
additional information
-
syrbactins, a family of natural products produced by strains of the plant pathogen Pseudomonas syringae pv. syringae, that belong either to the syringolin or glidobactin class, are highly potent proteasome inhibitors
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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%
-
nuclear factor erythroid-derived 2-related factor 1
-
i.e. Nrf1, a transcription factor of the cap and collar basic leucine zipper family, but not the related Nrf2, is necessary for induced proteasome gene transcription in cancer cell lines, overview
-
nuclear factor erythroid-derived 2-related factor 1
-
i.e. Nrf1, a transcription factor of the cap and collar basic leucine zipper family, but not the related Nrf2, is necessary for induced proteasome gene transcription in mouse embryonic fibroblasts, overview. Knockdown of Nrf1 in wild-type mouse embryonic fibroblasts abolishes MG132-mediated upregulation of RNA levels of PSM genes
-
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
-
SDS
-
stimulates chymotrypsin-like activity
SDS
-
stimulates peptidylglutamyl peptide hydrolase, branched-chain amino acid preferring and caseinolytic activities
SDS
-
stimulates chymotrypsin-like activity and Staphylococcus aureus V8 like activity
SDS
-
stimulates chymotrypsin-like activity, hydrolysis of benzyloxycarbonyl-GGL-4-nitroanilide and peptidyl-glutamyl-peptide-hydrolyzing activity, hydrolysis of benzyloxycarbonyl-LLE-2-naphthylamide
SDS
-
significantly stimulates activity of the 20S proteasome at pH 7.5, completely inhibits at pH 5.5
SDS
-
increased activity in the presence of 0.02% SDS
Leupeptin
-
0.05 mg/ml, activation to 125% of the original activity, peptidyl-glutamyl-peptide-hydrolyzing activity, hydrolysis of benzyloxycarbonyl-LLE-2-naphthylamide
additional information
-
occupancy of the caspase-like sites stimulates the trypsin-like activity of the proteasomes
-
additional information
-
immediate early gene-X-1 may essentially modulate signalling pathways related to 26S proteasome activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.032
acetyl-EPFD-7-amido-4-carbamoylcoumarin
-
pH 7.8, 25C
0.088
acetyl-EPFD-7-amido-4-carbamoylcoumarin
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
pH 7.8, 25C
0.36
acetyl-HHSL-7-amido-4-carbamoylcoumarin
-
pH 7.5, 25C
0.11
acetyl-norleucine-Arg-norleucine-Arg-7-amido-4-carbamoylcoumarin
-
pH 7.8, 25C
0.67
acetyl-norleucine-Arg-norleucine-Arg-7-amido-4-carbamoylcoumarin
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
pH 7.8, 25C
0.027
acetyl-YWTQ-7-amido-4-carbamoylcoumarin
-
pH 7.8, 25C
0.038
acetyl-YWTQ-7-amido-4-carbamoylcoumarin
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
pH 7.8, 25C
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
benzyloxycarbonyl-GPAFG-4-aminobenzoate
-
enzyme from spleen
0.8
benzyloxycarbonyl-GPAFG-4-aminobenzoate
-
enzyme from thymus
3.3
benzyloxycarbonyl-GPAFG-4-aminobenzoate
-
enzyme from pituitary
0.14
benzyloxycarbonyl-GPALG-4-aminobenzoate
-
enzyme from spleen
0.57
benzyloxycarbonyl-GPALG-4-aminobenzoate
-
enzyme from thymus
0.048
benzyloxycarbonyl-Leu-Leu-Leu-7-amido-4-methylcoumarin
-
-
0.255
benzyloxycarbonyl-LLE-2-naphthylamide
-
-
0.12
benzyloxycarbonyl-LLE-7-amino-4-methylcoumarin
-
-
0.051
benzyloxycarbonyl-RR-7-amido-4-methylcoumarin
-
-
0.01054
beta-casein
-
at 37C
-
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
-
-
0.07
succinyl-LLVY-7-amino-4-methylcoumarin
-
-
0.2
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.97
acetyl-EPFD-7-amido-4-carbamoylcoumarin
-
pH 7.8, 25C
2.7
acetyl-EPFD-7-amido-4-carbamoylcoumarin
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
pH 7.8, 25C
36.3
acetyl-HHSL-7-amido-4-carbamoylcoumarin
-
pH 7.5, 25C
0.031 - 0.51
acetyl-norleucine-Arg-norleucine-Arg-7-amido-4-carbamoylcoumarin
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
pH 7.8, 25C
3.3
acetyl-norleucine-Arg-norleucine-Arg-7-amido-4-carbamoylcoumarin
-
pH 7.8, 25C
5.34
acetyl-norleucine-Arg-norleucine-Arg-7-amido-4-carbamoylcoumarin
-
pH 7.8, 25C
8.15
acetyl-norleucine-Arg-norleucine-Arg-7-amido-4-carbamoylcoumarin
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
pH 7.8, 25C
0.27
acetyl-YWTQ-7-amido-4-carbamoylcoumarin
-
pH 7.8, 25C
3.3
acetyl-YWTQ-7-amido-4-carbamoylcoumarin
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
pH 7.8, 25C
4.67
acetyl-YWTQ-7-amido-4-carbamoylcoumarin
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
pH 7.8, 25C
2.94
benzyloxycarbonyl-ARR-7-amido-4-methylcoumarin
-
-
0.2
benzyloxycarbonyl-GGF-4-aminobenzoate
-
enzyme from thymus
16.9
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin
-
-
0.052 - 2.1
benzyloxycarbonyl-GGR-7-amido-4-methylcoumarin
-
-
1.98
benzyloxycarbonyl-GPAFG-4-aminobenzoate
-
enzyme from pituitary
2.94
benzyloxycarbonyl-GPAFG-4-aminobenzoate
-
enzyme from pituitary
3
benzyloxycarbonyl-GPAFG-4-aminobenzoate
-
enzyme from thymus
18.8
benzyloxycarbonyl-GPAFG-4-aminobenzoate
-
enzyme from spleen
0.03 - 0.55
benzyloxycarbonyl-GPALG-4-aminobenzoate
-
enzyme from thymus
0.5
benzyloxycarbonyl-GPALG-4-aminobenzoate
-
enzyme from spleen
3.75
benzyloxycarbonyl-GPALG-4-aminobenzoate
-
enzyme from pituitary
7.04
benzyloxycarbonyl-GPALG-4-aminobenzoate
-
enzyme from thymus
12.9
benzyloxycarbonyl-GPALG-4-aminobenzoate
-
enzyme from spleen
0.332
benzyloxycarbonyl-LLE-2-naphthylamide
-
-
6.08
succinyl-LLVY-7-amido-4-methylcoumarin
-
-
0.143
benzyloxycarbonyl-RR-7-amido-4-methylcoumarin
-
-
additional information
succinyl-AAF-7-amido-4-methylcoumarin
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
acetyl-Ala-Pro-norleucine-Leu-Asp-aldehyde
-
-
0.002
benzyloxycarbonyl-GPAF aldehyde
-
enzyme from thymus, substrate: benzyloxycarbonyl-GPALG-aminobenzoate
0.0026
benzyloxycarbonyl-GPAF aldehyde
-
enzyme from spleen, substrate: benzyloxycarbonyl-GPALG-aminobenzoate
0.00005
benzyloxycarbonyl-GPFL aldehyde
-
enzyme from thymus, substrate: benzyloxycarbonyl-GPAFG-p-aminobenzoate
0.00082
benzyloxycarbonyl-GPFL aldehyde
-
enzyme from thymus, substrate: benzyloxycarbonyl-GPALG-p-aminobenzoate
0.00104
benzyloxycarbonyl-GPFL aldehyde
-
enzyme from spleen, substrate: benzyloxycarbonyl-GPALG-p-aminobenzoate
0.00466
benzyloxycarbonyl-GPFL aldehyde
-
enzyme from pituitary, substrate: benzyloxycarbonyl-GPALG-p-aminobenzoate
0.00546
benzyloxycarbonyl-GPFL aldehyde
-
enzyme from thymus, substrate: benzyloxycarbonyl-GGF-p-aminobenzoate
0.0162
benzyloxycarbonyl-GPFL aldehyde
-
enzyme from spleen, substrate: benzyloxycarbonyl-GGF-p-aminobenzoate
0.0527
benzyloxycarbonyl-GPFL aldehyde
-
enzyme from pituitary, substrate: benzyloxycarbonyl-GGF-p-aminobenzoate
0.0016
benzyloxycarbonyl-LLF aldehyde
-
enzyme from pituitary, substrate: benzyloxycarbonyl-GGF-p-aminobenzoate
0.00251
benzyloxycarbonyl-LLF aldehyde
-
enzyme from thymus, substrate: benzyloxycarbonyl-GGF-p-aminobenzoate
0.00597
benzyloxycarbonyl-LLF aldehyde
-
enzyme from spleen, substrate: benzyloxycarbonyl-GGF-p-aminobenzoate
0.021
benzyloxycarbonyl-Pro-norleucine-Leu-Asp-aldehyde
-
-
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000086 - 0.000194
(-)-epigallocatechin-3-gallate
-
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)
-
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)
-
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)
-
pH 7.5, 30C
0.85
acetyl-Leu-Leu-Arg
-
IC50: 0.85 mM for chymotrypsin-like activity, 0.0056 mM for trypsin-like activity
0.11
benzyloxycarbonyl-Leu-Gly-Arg
-
IC50: 0.11 mM for chymotrypsin-like activity, 0.0066 mM for trypsin-like activity
0.056
Benzyloxycarbonyl-Leu-Leu-Arg
-
IC50: 0.056 mM for chymotrypsin-like activity, 0.0014 mM for trypsin-like activity
0.017
benzyloxycarbonyl-Leu-Ser-Arg
-
IC50: 0.017 mM for chymotrypsin-like activity, 0.0017 mM for trypsin-like activity
0.065
benzyloxycarbonyl-Leu-Thr-Arg
-
IC50: 0.065 mM for chymotrypsin-like activity, 0.0021 mM for trypsin-like activity
0.0089
benzyloxycarbonyl-Phe-Ser-Arg
-
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-)
-
inhibition of the chymotrypsin-like activity of the 20S proteasome
0.000049
glidobactin A
-
for the chymotrypsin-like activity, pH not specified in the publication, temperature not specified in the publication
0.002
glidobactin A
-
for the trypsin-like activity, pH not specified in the publication, temperature not specified in the publication
0.0347
KAuBr4
-
-
0.00084
N-(tert-butoxycarbonyl)-L-alanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N-(tert-butoxycarbonyl)-L-alanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
above, caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication; above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00428
N-(tert-butoxycarbonyl)-L-alanyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
-
chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N-(tert-butoxycarbonyl)-L-alanyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
-
above, caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication; above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.0015
N-(tert-butoxycarbonyl)-L-isoleucyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N-(tert-butoxycarbonyl)-L-isoleucyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
above, caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication; above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00147
N-(tert-butoxycarbonyl)-L-phenylalanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N-(tert-butoxycarbonyl)-L-phenylalanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
above, caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication; above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00054
N-(tert-butoxycarbonyl)glycyl-N1-benzyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-L-glutamamide
-
chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00984
N-(tert-butoxycarbonyl)glycyl-N1-benzyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-L-glutamamide
-
caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N-(tert-butoxycarbonyl)glycyl-N1-benzyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-L-glutamamide
-
above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00028
N-(tert-butoxycarbonyl)glycyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00854
N-(tert-butoxycarbonyl)glycyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N-(tert-butoxycarbonyl)glycyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00274
N-(tert-butoxycarbonyl)glycyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
-
chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N-(tert-butoxycarbonyl)glycyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
-
above, caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication; above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00785
N-[(1S)-1-benzyl-2-[[(1S)-1-(furan-2-ylcarbonyl)-3-methylbutyl]amino]-2-oxoethyl]-Na-(tert-butoxycarbonyl)-L-phenylalaninamide
-
-
0.00000865
N2-(decylcarbamoyl)-N-[(3E,5S,8S,9E)-2,7-dioxo-5-(propan-2-yl)-1,6-diazacyclododeca-3,9-dien-8-yl]-L-valinamide
-
for the chymotrypsin-like activity, pH not specified in the publication, temperature not specified in the publication
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
-
for the trypsin-like activity, pH not specified in the publication, temperature not specified in the publication
0.00451
N2-(tert-butoxycarbonyl)-N-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-3-[(naphthalen-2-ylmethyl)amino]-3-oxo-D-alaninamide
-
chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N2-(tert-butoxycarbonyl)-N-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-3-[(naphthalen-2-ylmethyl)amino]-3-oxo-D-alaninamide
-
above, caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication; above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00723
N2-(tert-butoxycarbonyl)-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N2-(tert-butoxycarbonyl)-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
above, chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication; above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00068
N2-(tert-butoxycarbonyl)-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
-
caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00412
N2-(tert-butoxycarbonyl)-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
-
chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N2-(tert-butoxycarbonyl)-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
-
above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.007
NPLLLVS
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
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
syringolin A
-
for the chymotrypsin-like activity, pH not specified in the publication, temperature not specified in the publication
0.0103
syringolin A
-
for the trypsin-like activity, pH not specified in the publication, temperature not specified in the publication
0.000757
syringolin A methyl ester
-
for the chymotrypsin-like activity, pH not specified in the publication, temperature not specified in the publication
-
0.0187
syringolin A methyl ester
-
for the trypsin-like activity, pH not specified in the publication, temperature not specified in the publication
-
0.00778
syringolin B
-
for the chymotrypsin-like activity, pH not specified in the publication, temperature not specified in the publication
0.1078
syringolin B
-
for the trypsin-like activity, pH not specified in the publication, temperature not specified in the publication
0.033
YLLLVS
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
0.1
Leupeptin
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
additional information
additional information
-
cell growth inhibition activities, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
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
-
-
29
-
chymotrypsin-like activity, KG1a cells, pH 7.4, 22C
71
-
chymotrypsin-like activity, U-937 cells, pH 7.4, 22C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
-
optimal cleavage of succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin
7
-
chymptrypsin-like and peptidylglutamyl peptide hydrolase activity
7.2
-
assay at
7.3
-
assay at
7.4
-
assay at
7.4
-
assay at
7.5
-
optimal cleavage of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
7.5
-
assay at
7.5
-
assay at
7.5
-
assay at
7.8 - 8.5
-
chymotrypsin-like activity, hydrolysis of benzyloxycarbonyl-GGL-4-nitroanilide and peptidyl-glutamyl-peptide-hydrolyzing activity, hydrolysis of benzyloxycarbonyl-LLE-2-naphthylamide
7.8
-
chymotrypsin-like activity
7.8
-
chymotrypsin-like activity
8
-
peptidylglutamyl peptide hydrolase activity
8
-
for trypsin-like activity
8
-
peptidylglutamyl peptide hydrolase activity
8
-
assay at
8
-
assay at
8.5
-
chymotrypsin-like activity
9
-
Staphylococcus aureus V8 like activity
9
-
trypsin-like activity, hydrolysis of benzyloxycarbonyl-GGR-2-naphthylamide
9
-
chymotryptic-like activity
10.5
-
trypsin-like activity
11
-
tryptic-like activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
assay at room temperature
22
-
in vivo assay at room temperature
30
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
in vitroo assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
40
-
tryptic-like activity
45
-
peptidylglutamyl peptide hydrolase activity
50
-
chymotrypsin-like and trypsin-like activities
60
-
chymotryptic-like activity
70
-
peptidylglutamyl peptide hydrolase activity
95
-
recombinant enzyme
119
-
wild-type enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80 - 100
-
80C: about 60% of maximal activity, 100C: about 45% of maximal activity, recombinant enzyme, hydrolysis of benzyloxycarbonyl-Ala-Ala-Leu-4-nitroanilide
100 - 130
-
100C: about 40% of maximal activity, 130C: about 20% of maximal activity, wild-type enzyme, hydrolysis of benzyloxycarbonyl-Ala-Ala-Leu-4-nitroanilide
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 7
-
subunits show pI-values from 4.5 to 7.0 by isoelectric focusing
4.7 - 4.8
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
subunit p54, theoretically determined by GENETYX-MAC 8.0
4.75
Q8I7N8
alpha5 subunit, predicted from amino acid sequence
4.93
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
subunit p110, theoretically determined by GENETYX-MAC 8.0
5.12
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
subunit p37A, theoretically determined by GENETYX-MAC 8.0
5.18
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
subunit p39A, theoretically determined by GENETYX-MAC 8.0
5.2
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
subunit p50, theoretically determined by GENETYX-MAC 8.0
5.22
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
subunit p48A, theoretically determined by GENETYX-MAC 8.0
5.48
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
subunit p97, theoretically determined by GENETYX-MAC 8.0
5.49
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
subunit p55, theoretically determined by GENETYX-MAC 8.0
5.66 - 6.17
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
subunit p42B, theoretically determined by GENETYX-MAC 8.0
5.74
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
subunit p37B, theoretically determined by GENETYX-MAC 8.0
5.75
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
subunit p48B, theoretically determined by GENETYX-MAC 8.0
5.8
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
subunit p30, theoretically determined by GENETYX-MAC 8.0
6.06
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
subunit p42A, theoretically determined by GENETYX-MAC 8.0
6.17
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
subunit P56, theoretically determined by GENETYX-MAC 8.0
8.44
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
subunit p42D, theoretically determined by GENETYX-MAC 8.0
8.51
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
subunit p42C, theoretically determined by GENETYX-MAC 8.0
8.9
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
subunit p39B, theoretically determined by GENETYX-MAC 8.0
9.04
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
subunit P58, theoretically determined by GENETYX-MAC 8.0
additional information
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
pI-values of the subunits
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
primary cells, and cell lines
Manually annotated by BRENDA team
-
from subjects with Alexander disease
Manually annotated by BRENDA team
-
differentiated from C6 glioma cells
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
differentiated from C6 glioma cells
-
Manually annotated by BRENDA team
-
immortalized with Epstein Barr virus
Manually annotated by BRENDA team
-
primary Waldenstroem macroglobulinemia cells
Manually annotated by BRENDA team
-
with lewy body disease
Manually annotated by BRENDA team
-
substantia nigra and putamen
Manually annotated by BRENDA team
-
proteasome composition in brain, overview
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
proteasome composition in brain, overview
-
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
-
localization in nuclei of neurons of the putamen and substantia nigra of Parkinson's disease patients, no nuclear localization is observed in the same areas of brains of controls
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
-
from fetal ICR mice
Manually annotated by BRENDA team
-
trypsin-like, the chymotrypsin-like, and the peptidyl-glutamyl peptide hydrolase activity of the 20S proteasome increase distinctly from freshly hatched larvae to pre-molt Z1. During the Z2 stage, the activities are highest in the post-molt animals, decrease in the inter-molt animals, and increase again in the pre-molt animals. A similar but less distinct trend is evident in the Z3 stages. In the juveniles, the proteasomal activities decrease toward the lowest values. A similar pattern is present for the chymotrypsin-like activity of the 26S proteasome
Manually annotated by BRENDA team
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
-
Manually annotated by BRENDA team
-
specific activities of the three standard proteasome subtypes II-2, II-3, and II-4 from rat heart exhibit high chymotrypsin-like activity, whereas the trypsin-like activity of these three subtypes account for only 1-2% compared with the chymotrypsin-like activity, their caspase-like activities overexceed the latter by 35-50%, overview
Manually annotated by BRENDA team
-
colon cancer cell line
Manually annotated by BRENDA team
-
of all three zoea stages Z1-Z3, as well as the first juvenile stage J1
Manually annotated by BRENDA team
-
proteolytic function of the 26S holoenzyme is involved in leaf polarity formation
Manually annotated by BRENDA team
-
tobacco mosaic virus-induced and salicylic acid-treated
Manually annotated by BRENDA team
-
prostate cancer cell line
Manually annotated by BRENDA team
-
prostate cancer cell line
Manually annotated by BRENDA team
-
fibroblast
Manually annotated by BRENDA team
-
a C57BL/6-derived methylcholantrene-induced fibrosarcoma cell line
Manually annotated by BRENDA team
-
breast cancer cell line
Manually annotated by BRENDA team
-
breast cancer cell
Manually annotated by BRENDA team
-
breast cancer cells
Manually annotated by BRENDA team
-
from peripheral blood
Manually annotated by BRENDA team
-
primary, multiple
Manually annotated by BRENDA team
-
neuroblastoma cell line
Manually annotated by BRENDA team
-
primary culture
Manually annotated by BRENDA team
-
localization in nuclei of neurons of the putamen and substantia nigra of Parkinson's disease patients, no nuclear localization is observed in the same areas of brains of controls
Manually annotated by BRENDA team
-
cortical neurons in primary culture from fetal ICR mice cerebral cortex
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
hippocampal
-
Manually annotated by BRENDA team
-
before vitellogenesis (up to stage 6), there is a continuous accumulation of the proteasomes in the nucleus of the oocyte. The outset of vitellogenesis is accompanied by a sharp decline in the nuclear accumulation of the proteasomes: in a majority of the stage 10 oocytes, only weak proteasome staining is seen. In the nucleus of about 30% of the oocytes the proteasome is barely detectable
Manually annotated by BRENDA team
-
pheochromocytoma cells
Manually annotated by BRENDA team
-
prostate cancer cell line
Manually annotated by BRENDA team
-
after germination, northern blot analysis
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
-
-
-
Manually annotated by BRENDA team
-
localization in nuclei of neurons of the putamen and substantia nigra of Parkinson's disease patients, no nuclear localization is observed in the same areas of brains of controls
Manually annotated by BRENDA team
-
osteosarcoma cell line
Manually annotated by BRENDA team
-
from subjects with Alexander disease, significantly decreased PGPH and chymotrypsin-like protease activities in white matter from Alexander disease patients expressing GFAP R239C, R416W, and R239H mutants
Manually annotated by BRENDA team
additional information
-
a higher proportion of doubly-capped 26S proteasome (19S-20S-19S) in the brain cortex than in the liver or kidney
Manually annotated by BRENDA team
additional information
-
not in gastric fluid
Manually annotated by BRENDA team
additional information
Rattus norvegicus Sprague-Dawley
-
a higher proportion of doubly-capped 26S proteasome (19S-20S-19S) in the brain cortex than in the liver or kidney
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
during the previtellogenic phase of oogenesis, the proteasomes are localized exclusively in the cytoplasm of the follicular cells. This is followed by a huge nuclear accumulation during the vitellogenic phase of oogenesis
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
-
mainly localized in the nucleus
Manually annotated by BRENDA team
-
during the previtellogenic phase of oogenesis, the proteasomes are localized exclusively in the cytoplasm of the follicular cells. This is followed by a huge nuclear accumulation during the vitellogenic phase of oogenesis
Manually annotated by BRENDA team
-
of neurons of the putamen and substantia nigra of Parkinson's disease patients, no nuclear localization is observed in the same areas of brains of controls
Manually annotated by BRENDA team
-
the 26S proteasome subunit RPN7 is localized in the nucleus
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26400
Q8I7N8
alpha5 subunit, predicted from amino acid sequence
684741
64000
-
gel filtration
649428
550000
-
SDS-PAGE
689687
630000
-
non-denaturing PAGE
137344
650000
-
gel filtration
137336
654000
-
gel filtration
137329
665000
-
non-denaturing PAGE
137351
690000
-
gel filtration
137346
700000
-
-
650467
700000
-
gel filtration
650902
850000
-
gel filtration
137335
894000
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
scanning transmission electron microscopy
652599
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
multimer
-
7 * ? (20S alpha-type subunits) + 10 * ? (20S beta-type subnits) + 16 * ? (19S ATPase subunits) + 14 * ? (19S non-ATPase subunits)
octadecamer
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61
1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
polymer
-
2 * alpah1-alpha7, beta1-beta7
polymer
-
alpha, beta, 14 * 24000 + 14 * 22000, SDS-PAGE, alpha7,beta7,beta7,alpha7 in the 20S proteasome
polymer
-
alpha, beta, 14 * 24000 + 14 * 22000, SDS-PAGE, alpha7,beta7,beta7,alpha7 in the 20S proteasome
tetradecamer
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
1 * 28000, alpha1, + 1 * 24300, alpha2, + 1 * 33000, alpha3, + 1 * 27000, alpha4, + 1 * 27500, alpha5, + 1 * 29000, alpha6, + 1 * 25000, alpha7, + 1 * 24700, beta1, + 1 * 24000, beta2, + 1 * 23200, beta3, + 1 * 23800, beta4, + 1 * 22700, beta5, + 1 * 24500, beta6, + 1 * 24000, beta7, the 20S proteasome is made up of seven alpha-subunits and seven beta-subunits. Of the seven beta-type subunits, five contain pro-sequences that are proteolytically removed during assembly, and three of them are predicted to be catalytic based on primary sequence
tetramer
-
alpha5-subunit PSMA5 exists as tetramer
heteromer
-
the 20S proteasomes are cylinder-shaped heteromeric dimers with a subunit configuration of alpha7, beta7, beta7, alpha7
additional information
-
multiple subunits from 21000-32000, SDS-PAGE
additional information
-
multiple subunits from 23000-115000, SDS-PAGE
additional information
-
multiple subunits from 22000-110000, SDS-PAGE
additional information
-
around 15 subunits from 20000-115000, SDS-PAGE
additional information
-
alpha, beta x * 27000 + x * 25000, SDS-PAGE
additional information
-
subunits from 20000-31000
additional information
-
x * 31000, x * 29000, x * 25000, x * 24000, tricine-SDS-PAGE
additional information
-
a ladder of 22200-33500 Da bands detected on SDS-PAGE
additional information
-
thre proteasomal subunits are identified as alpha6/Pre5, alpha3/Y13 and alpha5/Pup2 by internal sequencing of tryptic fragments. A fourth subunit is identified as alpha7/Prs1 by immunorecognition with a monoclonal antibody specific for C8
additional information
-
AE3 encodes the 26S proteasome lid subunit RPN8a that plays a role in specifying leaf adaxial identity
additional information
-
in the catalytic core, the 20S proteasome, the beta1, beta2 and beta5 subunits show peptidylglutamyl peptide hydrolyzing, trypsin-like and chymotrypsin-like activities, respectively. By INF-gamma and TNFalpha stimulus, these subunits are replaced by their counterparts LMP2, MECL-1 and LMP7, defined inducible subunits, thus originating the immunoproteasome
additional information
-
the tobacco mosaic virus-induced RNP7 subunit may be involved in programmed cell death
additional information
-
on 1-D SDS-PAGE five to seven bands of molecular weight range 20 to 30 kDa that prove to be entirely proteasome subunits, when the constituents are separated by 2-D SDS-PAGE, an unexpectedly large number of subunits is observed with at least 46 spots present versus an absolute minimum of 14 possible for a 20S core
additional information
-
in the 20S proteasome, the 20S core particle is composed of 28 subunits arranged in four stacked heptameric rings, alpha7beta7beta7alpha7, forming a symmetrical barrel-shaped structure. Determination of the subunits in proteasomal analysis, method optimization, overview
additional information
-
the 26 S proteasome is composed of two subparticles, the 20S core protease that compartmentalizes the protease active sites and the 19S regulatory particle that recognizes and translocates appropriate substrates into the core protease lumen for breakdown. The 2.5-MDa core protease-regulatory particle complex is actually a heterogeneous set of particles assembled with paralogous pairs for most subunits, mass spectrometric analysis of the complex, overview
additional information
-
three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings
additional information
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three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings. The archaeal alpha and beta rings are each composed of seven identical subunits, thus the archaeal 20S CP has true D7-symmetry
additional information
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three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings. The eukaryotic alpha and beta rings are each composed of seven distinct homologous subunits, which form a pseudo 7fold symmetrical structure of alpha1-7beta1-7beta1-7alpha1-7, with proteolytic active sites located at the N-termini of three subunits, beta1, beta2 and beta5, of each beta-ring. Another form of proteasome, called immunoproteasome, in which three beta-subunits of the normal 20S, beta1, beta2, beta5 are replaced by three IFN-gamma induced beta-subunits, beta1i, beta2i, beta5i. ATPase induced gate opening in the 20S CP
additional information
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three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings. The eukaryotic alpha and beta rings are each composed of seven distinct homologous subunits, which form a pseudo 7fold symmetrical structure of alpha17beta17beta17alpha17, with proteolytic active sites located at the N-termini of three subunits, beta1, beta2 and beta5, of each beta-ring
additional information
Arabidopsis thaliana Col-0
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the 26 S proteasome is composed of two subparticles, the 20S core protease that compartmentalizes the protease active sites and the 19S regulatory particle that recognizes and translocates appropriate substrates into the core protease lumen for breakdown. The 2.5-MDa core protease-regulatory particle complex is actually a heterogeneous set of particles assembled with paralogous pairs for most subunits, mass spectrometric analysis of the complex, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetylation
-
N-terminal acetylation of subunit alpha7
dephosphorylation
-
N-terminal dephosphorylation of subunit alpha7
proteolytic modification
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5
the 20S proteasome is made up of seven alpha-subunits and seven beta-subunits. Of the seven beta-type subunits, five contain pro-sequences that are proteolytically removed during assembly, and three of them are predicted to be catalytic based on primary sequence
additional information
-
a number of core and regulatory particle subunits undergo one or more posttranslational modifications, including partial proteolytic cleavage, acetylation, and ubiquitylation, mass spectrometric analysis of the complex, overview
additional information
Arabidopsis thaliana Col-0
-
a number of core and regulatory particle subunits undergo one or more posttranslational modifications, including partial proteolytic cleavage, acetylation, and ubiquitylation, mass spectrometric analysis of the complex, overview
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified 20S protease core, X-ray diffraction structure determination and analysis
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hanging drop vapour diffusion method, structure of the 20S proteasome/TMC-95A complex
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in complex with bortezomib, hanging drop vapour diffusion method at 24C in 30 mM MgOAc, 100 mM MES (pH 7.2), and 10% 2-methyl-2,4-pentanediol
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purified 20S protease core, X-ray diffraction structure determination and analysis
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vapor diffusion method
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crystal structure of the enzyme in complex with the competitive inhibitor acetyl-Leu-Leu-norleucinal
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purified 20S protease core, X-ray diffraction structure determination and analysis
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
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chymotrypsin-like and peptidylglutamyl peptide hydrolyzing activities increase, while trypsin-like activity decreases during cold exposure at 4C for 5-10 days
685897
40
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stable up to, trypsin-like activity
650467
60
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stable up to, chymotrypsin-like activity and peptidylglutamyl peptide hydrolase activity
650467
90 - 105
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a shift from 90 to 105C shows that the beta1 subunit gene of the 20S proteasome is up-regulated over twice within 5 min, the beta1 subunit in the 20S proteasome plays a thermostabilizing role and influences biocatalytic properties
687387
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Blm10 (a large protein known to attach to the alpha ring surface of proteasomes), the 19S regulatory particles, and the Pre4 C-terminal extension have partly redundant functions in 20S catalytic core particle formation and maturation
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the HEAT repeat protein Blm10 (a large protein known to attach to the alpha ring surface of proteasomes), the 19S regulatory particles, and the Pre4 C-terminal extension have partly redundant functions in 20S catalytic core particle formation and maturation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, in presence of ATP and glycerol, several months, no significant loss of activity
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4C, stable for up to 4 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
development of a method to purtify the 26S proteasome intact from whole Arabidopsis seedlings
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development of an affinity method to rapidly purify intact epitope-tagged 26S proteasomes using mutant homozygous PAG1-FLAG pag1-1 line
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DEAE-Toyopearl 650S column chromatography and Superose 6 gel filtration
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glutathione Sepharose 4B beads chromatography
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IgG-affinity resin chromatography
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Ni2+ chelate chromatography
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partially by preparation of erythrocytes, lysis, and differential centrifugation, determination of the subunits in proteasomal analysis, overview
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Q-Sepharose HP chromatography
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DEAE column chromatography, MonoQ HR5/5 column chromatography, and Superose 6 gel filtration
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native 20S proteasomes from hearts by ammonium sulfate fractionation, anion exchange chromatography, gel filtration, and hydrophobic interaction chromatography
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native 26S proteasomes from cytosolic or synaptosomal extracts of brain cortex by nickel and glutathione affinity chromatography
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Q Fast Flow column chromatography, Mono-Q column chromatography
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20S proteasome complex
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development of an integrated proteomic approach, QTAX, for quantitative analysis of tandem affinity purified in vivo cross-linked protein complexes to capture protein interactions of all natures in a single analysis, overview. Investigation of cell cycle specific proteasome interaction networks. Wild-type and RPN11-HBH cells are synchronized in three phases (G1, S, and M) before cross-linking and tandem affinity purification using nickel affinity resin and streptavidin beads after lysis using buffer containing 8 M urea, 300 mM NaCl, 50 mM NaH2PO4, 0.5% Igepal, 20 mM imidazole, and 1 mM PMSF, pH 8.5
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nickel affinity chromatography
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Superose 6 gel filtration and Superdex 200 gel filtration
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ammonium sulfate precipitation, Q-Sepharose column chromatography, CHTII hydroxyapatite column chromatography, and phenyl-Sepharose column chromatograpyh
-
Hiload 16/60 Superdex 200 gel filtration
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fungal 26S proteasome, comprising 102 distinct proteins, by anion exchange chromatography and gel filtration, method optimization, mass spectrometry and protein identifications, overview
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of the alpha-type subunit of the 20S catalytic core
-
26S proteasome subunits phylogenetic analysis
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expressed in Saccharomyces cerevisiae
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expressed in Hep-G2 cells
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expressed in 293 cell line
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expressed in Escherichia coli BL21 (DE3) cells and AH109 cells
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expressed in Jurkat cells
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PSMA5 is subcloned into the vector pET-22b(+) and expressed as inclusion bodies in Escherichia coli BL21
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expression in Escherichia coli
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expressed in MDA-MB-231 breast cancer cells
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expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
importance of antioxidant response elements in Nrf1-mediated upregulation of proteasome subunit genes
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ritonavir and A-792611 induce changes in the proteasome gene expression in rat liver, expression profiles, overview
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
identification of pag1-1, pa200-1-6, and T (transfer)-DNA insertion mutants in the Arabidopsis thaliana ecotype Col-0 in a T-DNA library, expression of HA-, Myc-, or FLAG-tagged PAG1 derivatives, gene At2g27020 or UniProt ID O23715. The PAG1-FLAG protein successfully integrated into the 26 S proteasome complex without perturbing CP/RP assembly or the phenotype
additional information
Arabidopsis thaliana Col-0
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identification of pag1-1, pa200-1-6, and T (transfer)-DNA insertion mutants in the Arabidopsis thaliana ecotype Col-0 in a T-DNA library, expression of HA-, Myc-, or FLAG-tagged PAG1 derivatives, gene At2g27020 or UniProt ID O23715. The PAG1-FLAG protein successfully integrated into the 26 S proteasome complex without perturbing CP/RP assembly or the phenotype
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additional information
-
Ubiquitinated proteins accumulate upon ectopic expression of S5aC. Ectopic S5a-UIM expression arrests cell cycle at G0 rather than at G2/M by epoxomicin. Downregulation of S5a by siRNA
additional information
-
construction of open-gated mutant, alpha3DELTAN 20S particles, that show much higher basal chymotrypsin-like activity compared with wild-type 20S activity, and are not inhibitable by prion protein isoforms, overview
additional information
-
development of an integrated proteomic approach, QTAX, for quantitative analysis of tandem affinity purified in vivo cross-linked protein complexes to capture protein interactions of all natures in a single analysis, overview. Investigation of cell cycle specific proteasome interaction networks. Wild-type and RPN11-HBH cells are synchronized in three phases (G1, S, and M) before cross-linking and tandem affinity purification
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
denaturation of the proteasome by 4 M urea followed by high-temperature dialysis. The wild-type temperature optimum is restored, but only if proteasome subunits are denatured and refolded prior to assembly
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
the incorporation of parus subunits into Arabidopsis holoprotease raises the intriguing possibility that plants synthesize multiple 26S proteasome types with unique properties and/or target specificities
drug development
-
the proteasome is a target for inhibitor development and optimization, overview
medicine
-
nuclear localization of 20S proteasome seems to be associated with the pathogeneses of Parkinson's disease
medicine
-
inhibitor development and optimization of the molecules can lead to better anticancer therapy, overview
medicine
-
Nrf1-mediated proteasome homeostasis can be an attractive target for therapeutic intervention in cancer
medicine
-
possible use of proteasome inhibitors for immunosuppression
medicine
-
proteasome inhibitors and other Hsp70 inducing agents may be useful in the treatment of a variety of genetic diseases caused by missense mutations
medicine
-
Nrf1-mediated proteasome homeostasis can be an attractive target for therapeutic intervention in cancer
biotechnology
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the 20S proteasome could be an as yet not identified bottleneck in the expression and secretion of some heterologous proteins by Streptomyces lividans. Optimization of the production of specific heterologous proteins is likely to require engineered Streptomyces lividans strains, in which the proteasome has been removed
medicine
-
proteasome inhibitors are used for the treatment of multiple myeloma and recurring mantle cell lymphoma, e.g. inhibitors MLN9708 and bortezomib, overview
additional information
-
peptide splicing is an intrinsic additional catalytic property of the proteasome, which may provide a qualitative peptide pool for immune selection