EC 3.4.25.1
- Proteasome endopeptidase complex
IntEnz Enzyme Nomenclature
EC 3.4.25.1
Names
Accepted name:
proteasome endopeptidase complex
Other
names:
26S protease
MCP
alkaline protease
ingensin
large multicatalytic protease
macropain
multicatalytic endopeptidase complex
multicatalytic proteinase
multicatalytic proteinase (complex)
prosome
proteasome
proteasome organelle
tricorn protease
tricorn proteinase
Reaction
-
Cleavage of peptide bonds with very broad specificity.
Comments:
A 20-S protein composed of 28 subunits arranged in four rings of seven. The outer rings are composed of a subunits, but the b subunits forming the inner rings are responsible for peptidase activity. In eukaryotic organisms there are up to seven different types of b subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities. The molecule is barrel-shaped, and the active sites are on the inner surfaces. Terminal apertures restrict access of substrates to the active sites. There is evidence that catalytic subunits are replaced by others under some conditions so as to alter the specificity of proteolysis, perhaps optimizing it for the formation of antigenic peptides. A complex of the 20-S proteasome endopeptidase complex with a 19-S regulatory unit is the 26-S proteasome that degrades ubiquitin-protein conjugates. Type example of peptidase family T1. Formerly EC 3.4.24.5, EC 3.4.22.21 and EC 3.4.99.46.
Links to other databases
CAS Registry Number:
140879-24-9
INPE_EMENI
PB6LA_SALSA
PB6LB_SALSA
PBS5_CAEEL
PSB10_BOVIN
PSB10_HUMAN
PSB10_MOUSE
PSB10_RAT
PSB11_HUMAN
PSB11_MOUSE
PSB1_AERPE
PSB1_CALMQ
PSB1_CENSY
PSB1_DESA1
PSB1_ENCCU
PSB1_HALMA
PSB1_HALTV
PSB1_HYPBU
PSB1_IGNH4
PSB1_KORCO
PSB1_METS5
PSB1_NITMS
PSB1_PYRAB
PSB1_PYRAE
PSB1_PYRAR
PSB1_PYRCJ
PSB1_PYRFU
PSB1_PYRHO
PSB1_PYRIL
PSB1_PYRNV
PSB1_RHOER
PSB1_SACS2
PSB1_SACS9
PSB1_SALTO
PSB1_SCHPO
PSB1_STAMF
PSB1_STRAW
PSB1_SULAC
PSB1_SULIA
PSB1_SULID
PSB1_SULIK
PSB1_SULIL
PSB1_SULIM
PSB1_SULIN
PSB1_SULIY
PSB1_SULTO
PSB1_THECD
PSB1_THEGJ
PSB1_THEKO
PSB1_THEON
PSB1_THEPD
PSB1_THESM
PSB1_YEAST
PSB2_AERPE
PSB2_CALMQ
PSB2_CENSY
PSB2_DESA1
PSB2_ENCCU
PSB2_HALMA
PSB2_HALTV
PSB2_HYPBU
PSB2_IGNH4
PSB2_KORCO
PSB2_METS5
PSB2_NITMS
PSB2_PYRAB
PSB2_PYRAE
PSB2_PYRAR
PSB2_PYRCJ
PSB2_PYRFU
PSB2_PYRHO
PSB2_PYRIL
PSB2_PYRNV
PSB2_RHOER
PSB2_SACS2
PSB2_SACS9
PSB2_SALTO
PSB2_SCHPO
PSB2_STAMF
PSB2_STRAW
PSB2_SULAC
PSB2_SULIA
PSB2_SULID
PSB2_SULIK
PSB2_SULIL
PSB2_SULIM
PSB2_SULIN
PSB2_SULIY
PSB2_SULTO
PSB2_THECD
PSB2_THEGJ
PSB2_THEKO
PSB2_THEON
PSB2_THEPD
PSB2_THESM
PSB2_YEAST
PSB5-2_HUMAN
PSB5-3_HUMAN
PSB5A_ARATH
PSB5B_ARATH
PSB5_BOVIN
PSB5_CHICK
PSB5_DICDI
PSB5_HUMAN
PSB5_MOUSE
PSB5_PONAB
PSB5_RAT
PSB5_SCHPO
PSB5_SPIOL
PSB5_YEAST
PSB6_ARATH
PSB6_BOVIN
PSB6_DICDI
PSB6_HUMAN
PSB6_MOUSE
PSB6_RAT
PSB6_TOBAC
PSB7-2_HUMAN
PSB7A-2_ARATH
PSB7A_ARATH
PSB7B_ARATH
PSB7_BOVIN
PSB7_DICDI
PSB7_HUMAN
PSB7_MOUSE
PSB7_PIG
PSB7_RAT
PSB8-2_HUMAN
PSB8_BOVIN
PSB8_CANLF
PSB8_HUMAN
PSB8_MOUSE
PSB8_PIG
PSB8_RAT
PSB9-2_HUMAN
PSB9_BOVIN
PSB9_HUMAN
PSB9_MOUSE
PSB9_MUSMB
PSB9_MUSPL
PSB9_MUSSI
PSB9_MUSTR
PSB9_ONCMY
PSB9_ORYLA
PSB9_RAT
PSB9_SALSA
PSB_ACIB4
PSB_ACIC1
PSB_ACIFD
PSB_ACTMD
PSB_ARCFU
PSB_ARCPA
PSB_ARTS2
PSB_BEUC1
PSB_CATAD
PSB_FERPA
PSB_FRAAA
PSB_FRACC
PSB_FRASN
PSB_GEOOG
PSB_GORB4
PSB_HALLT
PSB_HALMD
PSB_HALS3
PSB_HALSA
PSB_HALUD
PSB_HALVD
PSB_HALWD
PSB_JONDD
PSB_KINRD
PSB_KRIFD
PSB_META3
PSB_METAC
PSB_METAR
PSB_METB6
PSB_METBF
PSB_METBU
PSB_METFA
PSB_METHJ
PSB_METJA
PSB_METKA
PSB_METLZ
PSB_METM5
PSB_METM6
PSB_METM7
PSB_METMA
PSB_METMJ
PSB_METMP
PSB_METMS
PSB_METPE
PSB_METPS
PSB_METRM
PSB_METS3
PSB_METSF
PSB_METST
PSB_METTE
PSB_METTH
PSB_METTP
PSB_METVM
PSB_METVS
PSB_MYCA1
PSB_MYCA9
PSB_MYCBO
PSB_MYCBP
PSB_MYCBT
PSB_MYCGI
PSB_MYCLB
PSB_MYCLE
PSB_MYCMM
PSB_MYCPA
PSB_MYCS2
PSB_MYCSJ
PSB_MYCSK
PSB_MYCSS
PSB_MYCTA
PSB_MYCTF
PSB_MYCTK
PSB_MYCTO
PSB_MYCTU
PSB_MYCUA
PSB_MYCVP
PSB_NAKMY
PSB_NANEQ
PSB_NATMM
PSB_NATPD
PSB_NOCFA
PSB_NOCSJ
PSB_PAEAT
PSB_PICTO
PSB_PSECP
PSB_RENSM
PSB_RHOE4
PSB_RHOJR
PSB_RHOOB
PSB_SACEN
PSB_SACVD
PSB_SALAI
PSB_SANKS
PSB_STANL
PSB_STRCO
PSB_STRGG
PSB_STRRD
PSB_STRSW
PSB_THEAC
PSB_THEFY
PSB_THEVO
PSB_XYLCX
References
-
Seemüller, E., Lupas, A., Stock, D., Löwe, J., Huber, R. and Baumeister, W.
Proteasome from Thermoplasma acidophilum: a threonine protease.
Science
268
:
579-582
(1995).
[PMID:
7725107]
-
Coux, O., Tanaka, K. and Goldberg, A.L.
Structure and functions of the 20S and 26S proteasomes.
Annu. Rev. Biochem.
65
:
801-847
(1996).
[PMID:
8811196]
-
Groll, M., Ditzel, L., Löwe, J., Stock, D., Bochtler, M., Bartunik, H.D. and Huber, R.
Structure of 20S proteasome from yeast at 2.4Å resolution.
Nature
386
:
463-471
(1997).
[PMID:
9087403]
-
Dick, T.P., Nussbaum, A.K., Deeg, M., Heinemeyer, W., Groll, M., Schirle, M., Keilholz, W., Stevanovic, S., Wolf, D.H., Huber, R., Rammensee, H.G. and Schild, H.
Contribution of proteasomal β-subunits to the cleavage of peptide substrates analyzed with yeast mutants.
J. Biol. Chem.
386
:
25637-25646
(1998).
[PMID:
9748229]
[EC 3.4.25.1 created 1978 as EC 3.4.24.5, part transferred 1989 to EC 3.4.22.21, transferred 1992 to EC 3.4.99.46, transferred 2000 to EC 3.4.25.1]