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Information on EC 3.4.25.1 - proteasome endopeptidase complex and Organism(s) Arabidopsis thaliana

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This record set is specific for:
Arabidopsis thaliana
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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cleavage of peptide bonds with very broad specificity
Synonyms
proteasome, 26s proteasome, 20s proteasome, 26 s proteasome, multicatalytic proteinase, 20 s proteasome, multicatalytic protease, 26s proteasome complex, prosome, proteasome 20s, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
206 proteasome
-
the 26S proteasome is composed of the 20S and the 19S complex
26S protease
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-
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27 kDa prosomal protein
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-
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30 kDa prosomal protein
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Component Y8
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-
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GPRO-28
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-
-
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HsBPROS26
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-
-
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HSN3
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-
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ingensin
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large multicatalytic protease
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-
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macropain
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-
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multicatalytic endopeptidase complex
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-
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Multicatalytic endopeptidase complex C7
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multicatalytic protease
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multicatalytic proteinase
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-
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p27K
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-
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PROS-27
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PROS-30
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-
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PROS-Dm25
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PROS-Dm28.1
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-
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PROS-Dm29
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-
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PROS-Dm35
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prosome
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-
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proteasome
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Proteasome component C13
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Proteasome component C2
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Proteasome component C3
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Proteasome component C5
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Proteasome component C8
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Proteasome component C9
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Proteasome component DD4
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Proteasome component DD5
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Proteasome component pts1
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RING12 protein
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RN3
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SCL1 suppressor protein
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TAS-F22/FAFP98
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-
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TAS-G64
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TCPR29
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tricorn protease
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tricorn proteinase
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XC3
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
140879-24-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-aminocyclopropane-1-carboxylic acid synthase 6 + H2O
?
show the reaction diagram
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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
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-
?
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
Boc-Leu-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
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trypsin-like activity
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-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
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-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
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?
additional information
?
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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
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
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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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
epoxomicin
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lactacystin
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MG132
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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proteolytic function of the 26S holoenzyme is involved in leaf polarity formation
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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T-DNA insertion mutation in RPN1a results in increased trichome branches on main stem, and trichome number on rosette leaves and the main stem compared with the wild type plant
physiological function
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the RPN1a subunit of the 26S proteasome is involved in trichome's branching in Arabidopsis thaliana through the giberellin and cytokinin signaling pathways
additional information
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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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PSB6_ARATH
233
0
25151
Swiss-Prot
other Location (Reliability: 2)
PSB7A_ARATH
273
0
29555
Swiss-Prot
other Location (Reliability: 1)
PSB7B_ARATH
274
0
29617
Swiss-Prot
other Location (Reliability: 2)
PSB5A_ARATH
274
0
29668
Swiss-Prot
other Location (Reliability: 2)
PSB5B_ARATH
273
0
29485
Swiss-Prot
other Location (Reliability: 2)
F4KIN7_ARATH
268
0
28959
TrEMBL
other Location (Reliability: 2)
F4IWI5_ARATH
267
0
28897
TrEMBL
other Location (Reliability: 2)
A0A7G2F214_ARATH
390
0
43634
TrEMBL
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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
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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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
26S proteasome subunits phylogenetic analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the mRNA expression level of subunit RPN1a is significantly repressed by gibberellin and cytokinin treatment
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yang, P.; Fu, H.; Walker, J.; Papa, C.M.; Smalle, J.; Ju, Y.; Vierstra, R.D.
Purification of the Arabidopsis 26 S proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms
J. Biol. Chem.
279
6401-6413
2004
Arabidopsis thaliana
Manually annotated by BRENDA team
Huang, W.; Pi, L.; Liang, W.; Xu, B.; Wang, H.; Cai, R.; Huang, H.
The proteolytic function of the Arabidopsis 26S proteasome is required for specifying leaf adaxial identity
Plant Cell
18
2479-2492
2006
Arabidopsis thaliana
Manually annotated by BRENDA team
Joo, S.; Liu, Y.; Lueth, A.; Zhang, S.
MAPK phosphorylation-induced stabilization of ACS6 protein is mediated by the non-catalytic C-terminal domain, which also contains the cis-determinant for rapid degradation by the 26S proteasome pathway
Plant J.
54
129-140
2008
Arabidopsis thaliana
Manually annotated by BRENDA team
Book, A.J.; Gladman, N.P.; Lee, S.S.; Scalf, M.; Smith, L.M.; Vierstra, R.D.
Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse array of plant proteolytic complexes
J. Biol. Chem.
285
25554-25569
2010
Arabidopsis thaliana, Arabidopsis thaliana Col-0
Manually annotated by BRENDA team
Yu, D.; Yu, F.; Du, C.; Li, X.; Zhao, X.; Liu, X.
RPN1a, a subunit of the 26S proteasome, controls trichome development in Arabidopsis
Plant Physiol. Biochem.
88
82-88
2015
Arabidopsis thaliana
Manually annotated by BRENDA team