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Information on EC 3.4.25.1 - proteasome endopeptidase complex

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UNIPROT: P21243 not found.
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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
20S CP
core particle of the proteasome 20S
26S protease
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27 kDa prosomal protein
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30 kDa prosomal protein
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Component Y8
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GPRO-28
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HsBPROS26
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HSN3
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ingensin
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large multicatalytic protease
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macropain
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multicatalytic endopeptidase complex
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Multicatalytic endopeptidase complex C7
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multicatalytic protease
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multicatalytic proteinase
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p27K
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PROS-27
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PROS-30
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PROS-Dm25
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PROS-Dm28.1
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PROS-Dm29
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PROS-Dm35
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prosome
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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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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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PSA1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
252
0
28001
Swiss-Prot
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PDB
SCOP
CATH
UNIPROT
ORGANISM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cryo-EM structures of the actively ATP-hydrolyzing, substrate-engaged 26S proteasome with four distinct motor conformations. Structures suggest a ubiquitin capture mechanism, in which mechanical pulling on the substrate by the AAA+ motor delivers ubiquitin modifications directly into the Rpn11 catalytic groove and accelerates isopeptide cleavage for efficient, cotranslocational deubiquitination. The substrate polypeptide traverses from the Rpn11 deubiquitinase, through the AAA+ motor, and into the core peptidase. The proteasomal motor thereby adopts staircase arrangements with five substrate-engaged subunits and one disengaged subunit. Four of the substrate-engaged subunits are ATP bound, whereas the subunit at the bottom of the staircase and the disengaged subunit are bound to ADP
enzyme core particle with the alpha7DELTAN mutation, hanging drop vapor diffusion method, using 0.1 M MES (pH 6.5), 50 mM magnesium acetate, and 14% (v/v) 2-methyl-2,4-pentanediol
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
anti-Flag M2 agarose bead chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yashiroda, H.; Toda, Y.; Otsu, S.; Takagi, K.; Mizushima, T.; Murata, S.
N-terminal alpha7 deletion of the proteasome 20S core particle substitutes for yeast PI31 function
Mol. Cell. Biol.
35
141-152
2015
Saccharomyces cerevisiae (P21243), Saccharomyces cerevisiae
Manually annotated by BRENDA team
de la Pena, A.H.; Goodall, E.A.; Gates, S.N.; Lander, G.C.; Martin, A.
Substrate-engaged 26S proteasome structures reveal mechanisms for ATP-hydrolysis-driven translocation
Science
362
6418
2018
Saccharomyces cerevisiae (P21243)
Manually annotated by BRENDA team