DB code: M00174
| RLCP classification | 1.13.30010.35 : Hydrolysis | |
|---|---|---|
| CATH domain | 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | |
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | ||
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | ||
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | ||
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | ||
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | ||
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | ||
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | ||
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | ||
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | ||
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | ||
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | ||
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | ||
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | ||
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | Catalytic domain | |
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | Catalytic domain | |
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | Catalytic domain | |
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | Catalytic domain | |
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | Catalytic domain | |
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | Catalytic domain | |
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | Catalytic domain | |
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | Catalytic domain | |
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | Catalytic domain | |
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | Catalytic domain | |
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | Catalytic domain | |
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | Catalytic domain | |
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | Catalytic domain | |
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | Catalytic domain | |
| E.C. | 3.4.25.1 | |
| CSA | 1pma | |
| M-CSA | 1pma | |
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 | T00201 M00123 D00300 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam | MEROPS |
|---|---|---|---|---|---|
| P25156 |
Proteasome subunit alpha
|
EC
3.4.25.1
Multicatalytic endopeptidase complex subunit alpha |
NP_394744.1
(Protein)
NC_002578.1 (DNA/RNA sequence) |
PF00227
(Proteasome)
PF10584 (Proteasome_A_N) [Graphical View] |
|
| P28061 |
Proteasome subunit beta
|
EC
3.4.25.1
Multicatalytic endopeptidase complex subunit beta |
NP_394085.1
(Protein)
NC_002578.1 (DNA/RNA sequence) |
PF00227
(Proteasome)
[Graphical View] |
T01.002
(Threonine)
|
| KEGG enzyme name |
|---|
|
proteasome endopeptidase complex
ingensin macropain multicatalytic endopeptidase complex prosome multicatalytic proteinase (complex) MCP proteasome large multicatalytic protease multicatalytic proteinase proteasome organelle alkaline protease 26S protease tricorn proteinase tricorn protease |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P25156 | PSMA_THEAC | Cleavage of peptide bonds with very broad specificity. | Composed of two subunits, alpha and beta. The complex is formed of four rings. The two outer rings are each composed of seven alpha subunits. The two inner rings are each composed of seven beta subunits. | Cytoplasm. | |
| P28061 | PSMB_THEAC | Cleavage of peptide bonds with very broad specificity. | Composed of two subunits, alpha and beta. The complex is formed of four rings. The two outer rings are each composed of seven alpha subunits. The two inner rings are each composed of seven beta subunits. | Cytoplasm. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|
| Compound table | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Substrates | Products | Intermediates | |||||||||
| KEGG-id | C00017 | C00012 | C00001 | C00017 | C00012 | ||||||
| E.C. | |||||||||||
| Compound | Protein | Peptide | H2O | Protein | Peptide | ||||||
| Type | peptide/protein | peptide/protein | H2O | peptide/protein | peptide/protein | ||||||
| ChEBI |
15377 15377 |
||||||||||
| PubChem |
22247451 962 22247451 962 |
||||||||||
| 1pmaA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaC |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaD |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaE |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaF |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaG |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaH |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaI |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaJ |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaK |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaL |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaM |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaN |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaO |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ya7A |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ya7B |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ya7C |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ya7D |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ya7E |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ya7F |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ya7G |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yarA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yarB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yarC |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yarD |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yarE |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yarF |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yarG |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yauA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yauB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yauC |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yauD |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yauE |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yauF |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yauG |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaP |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaQ |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaR |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaS |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaT |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaU |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaV |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaW |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaX |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaY |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pmaZ |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pma1 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1pma2 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ya7H |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ya7I |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ya7J |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ya7K |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ya7L |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ya7M |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1ya7N |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yarH |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yarI |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yarJ |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yarK |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yarL |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yarM |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yarN |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yauH |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yauI |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yauJ |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yauK |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yauL |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yauM |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1yauN |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1pmaA |
|
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|||||
| 1pmaC |
|
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|
|||||
| 1pmaD |
|
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|
|||||
| 1pmaE |
|
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|||||
| 1pmaF |
|
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|
|||||
| 1pmaG |
|
|
|
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|||||
| 1pmaH |
|
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|
|||||
| 1pmaI |
|
|
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|
|||||
| 1pmaJ |
|
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|
|||||
| 1pmaK |
|
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|
|||||
| 1pmaL |
|
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|
|||||
| 1pmaM |
|
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|
|
|
|||||
| 1pmaN |
|
|
|
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|
|||||
| 1pmaO |
|
|
|
|
|
|||||
| 1ya7A |
|
|
|
|
|
|||||
| 1ya7B |
|
|
|
|
|
|||||
| 1ya7C |
|
|
|
|
|
|||||
| 1ya7D |
|
|
|
|
|
|||||
| 1ya7E |
|
|
|
|
|
|||||
| 1ya7F |
|
|
|
|
|
|||||
| 1ya7G |
|
|
|
|
|
|||||
| 1yarA |
|
|
|
|
|
|||||
| 1yarB |
|
|
|
|
|
|||||
| 1yarC |
|
|
|
|
|
|||||
| 1yarD |
|
|
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|
|||||
| 1yarE |
|
|
|
|
|
|||||
| 1yarF |
|
|
|
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|
|||||
| 1yarG |
|
|
|
|
|
|||||
| 1yauA |
|
|
|
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|
|||||
| 1yauB |
|
|
|
|
|
|||||
| 1yauC |
|
|
|
|
|
|||||
| 1yauD |
|
|
|
|
|
|||||
| 1yauE |
|
|
|
|
|
|||||
| 1yauF |
|
|
|
|
|
|||||
| 1yauG |
|
|
|
|
|
|||||
| 1pmaB |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1pmaP |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1pmaQ |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1pmaR |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1pmaS |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1pmaT |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1pmaU |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1pmaV |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1pmaW |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1pmaX |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1pmaY |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1pmaZ |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1pma1 |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1pma2 |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1ya7H |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1ya7I |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1ya7J |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1ya7K |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1ya7L |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1ya7M |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1ya7N |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1yarH |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1yarI |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1yarJ |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1yarK |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1yarL |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1yarM |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1yarN |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1yauH |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1yauI |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1yauJ |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1yauK |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1yauL |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1yauM |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| 1yauN |
|
|
|
|
|
THR 1;GLU 17;LYS 33;ASP 166 | THR 1;GLY 47 | |||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[3]
|
Fig.4, p.517-519 | |
|
[4]
|
Fig.5A, p.529-530 | |
|
[11]
|
p.418 | |
|
[13]
|
p.381-382 | |
|
[16]
|
p.275-276 | |
|
[18]
|
Fig.2, p.4-5 | |
|
[19]
|
p.840-841 | |
|
[20]
|
Fig.2 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7697124 |
| Journal | Enzyme Protein |
| Year | 1993 |
| Volume | 47 |
| Pages | 252-73 |
| Authors | Lupas A, Koster AJ, Baumeister W |
| Title | Structural features of 26S and 20S proteasomes. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7697123 |
| Journal | Enzyme Protein |
| Year | 1993 |
| Volume | 47 |
| Pages | 241-51 |
| Authors | Tanahashi N, Tsurumi C, Tamura T, Tanaka K |
| Title | Molecular structure of 20S and 26S proteasomes. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8824424 |
| Journal | Cold Spring Harb Symp Quant Biol |
| Year | 1995 |
| Volume | 60 |
| Pages | 515-24 |
| Authors | Lupas A, Zwickl P, Wenzel T, Seemuller E, Baumeister W |
| Title | Structure and function of the 20S proteasome and of its regulatory complexes. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8824425 |
| Journal | Cold Spring Harb Symp Quant Biol |
| Year | 1995 |
| Volume | 60 |
| Pages | 525-32 |
| Authors | Stock D, Ditzel L, Baumeister W, Huber R, Lowe J |
| Title | Catalytic mechanism of the 20S proteasome of Thermoplasma acidophilum revealed by X-ray crystallography. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7867793 |
| Journal | FEBS Lett |
| Year | 1995 |
| Volume | 359 |
| Pages | 173-8 |
| Authors | Seemuller E, Lupas A, Zuhl F, Zwickl P, Baumeister W |
| Title | The proteasome from Thermoplasma acidophilum is neither a cysteine nor a serine protease. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7565658 |
| Journal | Mol Biol Rep |
| Year | 1995 |
| Volume | 21 |
| Pages | 11-20 |
| Authors | Koster AJ, Walz J, Lupas A, Baumeister W |
| Title | Structural features of archaebacterial and eukaryotic proteasomes. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7477383 |
| Journal | Nature |
| Year | 1995 |
| Volume | 378 |
| Pages | 416-9 |
| Authors | Brannigan JA, Dodson G, Duggleby HJ, Moody PC, Smith JL, Tomchick DR, Murzin AG |
| Title | A protein catalytic framework with an N-terminal nucleophile is capable of self-activation. |
| Related PDB | |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7725095 |
| Journal | Science |
| Year | 1995 |
| Volume | 268 |
| Pages | 522-3 |
| Authors | Goldberg AL |
| Title | Functions of the proteasome: the lysis at the end of the tunnel. |
| Related PDB | |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7725097 |
| Journal | Science |
| Year | 1995 |
| Volume | 268 |
| Pages | 533-9 |
| Authors | Lowe J, Stock D, Jap B, Zwickl P, Baumeister W, Huber R |
| Title |
Crystal structure of the 20S proteasome from the archaeon T. |
| Related PDB | 1pma |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7725107 |
| Journal | Science |
| Year | 1995 |
| Volume | 268 |
| Pages | 579-82 |
| Authors | Seemuller E, Lupas A, Stock D, Lowe J, Huber R, Baumeister W |
| Title | Proteasome from Thermoplasma acidophilum: a threonine protease. |
| Related PDB | |
| Related UniProtKB | |
| [11] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7663937 |
| Journal | Structure |
| Year | 1995 |
| Volume | 3 |
| Pages | 417-20 |
| Authors | Wlodawer A |
| Title | Proteasome: a complex protease with a new fold and a distinct mechanism. |
| Related PDB | |
| Related UniProtKB | |
| [12] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8811196 |
| Journal | Annu Rev Biochem |
| Year | 1996 |
| Volume | 65 |
| Pages | 801-47 |
| Authors | Coux O, Tanaka K, Goldberg AL |
| Title | Structure and functions of the 20S and 26S proteasomes. |
| Related PDB | |
| Related UniProtKB | |
| [13] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8768894 |
| Journal | Curr Opin Biotechnol |
| Year | 1996 |
| Volume | 7 |
| Pages | 376-85 |
| Authors | Stock D, Nederlof PM, Seemuller E, Baumeister W, Huber R, Lowe J |
| Title | Proteasome: from structure to function. |
| Related PDB | |
| Related UniProtKB | |
| [14] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8684489 |
| Journal | Nature |
| Year | 1996 |
| Volume | 382 |
| Pages | 468-71 |
| Authors | Seemuller E, Lupas A, Baumeister W |
| Title | Autocatalytic processing of the 20S proteasome. |
| Related PDB | |
| Related UniProtKB | |
| [15] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9377486 |
| Journal | Biol Chem |
| Year | 1997 |
| Volume | 378 |
| Pages | 893-8 |
| Authors | Escherich A, Ditzel L, Musiol HJ, Groll M, Huber R, Moroder L |
| Title |
Synthesis, |
| Related PDB | |
| Related UniProtKB | |
| [16] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9094332 |
| Journal | Curr Opin Struct Biol |
| Year | 1997 |
| Volume | 7 |
| Pages | 273-8 |
| Authors | Baumeister W, Lupas A |
| Title | The proteasome. |
| Related PDB | |
| Related UniProtKB | |
| [17] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9334174 |
| Journal | J Biol Chem |
| Year | 1997 |
| Volume | 272 |
| Pages | 26103-9 |
| Authors | Mc Cormack T, Baumeister W, Grenier L, Moomaw C, Plamondon L, Pramanik B, Slaughter C, Soucy F, Stein R, Zuhl F, Dick L |
| Title |
Active site-directed inhibitors of Rhodococcus 20 S proteasome. |
| Related PDB | |
| Related UniProtKB | |
| [18] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11097171 |
| Journal | Arch Biochem Biophys |
| Year | 2000 |
| Volume | 383 |
| Pages | 1-16 |
| Authors | Orlowski M, Wilk S |
| Title |
Catalytic activities of the 20 S proteasome, |
| Related PDB | |
| Related UniProtKB | |
| [19] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10966872 |
| Journal | Front Biosci |
| Year | 2000 |
| Volume | 5 |
| Pages | D837-65 |
| Authors | Maupin-Furlow JA, Wilson HL, Kaczowka SJ, Ou MS |
| Title | Proteasomes in the archaea: from structure to function. |
| Related PDB | |
| Related UniProtKB | |
| [20] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10809725 |
| Journal | J Biol Chem |
| Year | 2000 |
| Volume | 275 |
| Pages | 14831-7 |
| Authors | Kisselev AF, Songyang Z, Goldberg AL |
| Title |
Why does threonine, |
| Related PDB | |
| Related UniProtKB | |
| [21] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10843865 |
| Journal | J Mol Biol |
| Year | 2000 |
| Volume | 299 |
| Pages | 1147-54 |
| Authors | Gille C, Goede A, Preissner R, Rother K, Frommel C |
| Title | Conservation of substructures in proteins: interfaces of secondary structural elements in proteasomal subunits. |
| Related PDB | |
| Related UniProtKB | |
| [22] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12083009 |
| Journal | Curr Top Microbiol Immunol |
| Year | 2002 |
| Volume | 268 |
| Pages | 73-89 |
| Authors | Hill CP, Masters EI, Whitby FG |
| Title | The 11S regulators of 20S proteasome activity. |
| Related PDB | |
| Related UniProtKB | |
| [23] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12083007 |
| Journal | Curr Top Microbiol Immunol |
| Year | 2002 |
| Volume | 268 |
| Pages | 23-41 |
| Authors | Zwickl P |
| Title | The 20S proteasome. |
| Related PDB | |
| Related UniProtKB | |
| [24] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12354607 |
| Journal | FEBS Lett |
| Year | 2002 |
| Volume | 529 |
| Pages | 22-6 |
| Authors | Dantuma NP, Masucci MG |
| Title | Stabilization signals: a novel regulatory mechanism in the ubiquitin/proteasome system. |
| Related PDB | |
| Related UniProtKB | |
| [25] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12941688 |
| Journal | EMBO J |
| Year | 2003 |
| Volume | 22 |
| Pages | 4356-64 |
| Authors | Forster A, Whitby FG, Hill CP |
| Title | The pore of activated 20S proteasomes has an ordered 7-fold symmetric conformation. |
| Related PDB | |
| Related UniProtKB | |
| [26] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12614609 |
| Journal | J Mol Biol |
| Year | 2003 |
| Volume | 327 |
| Pages | 75-83 |
| Authors | Groll M, Brandstetter H, Bartunik H, Bourenkow G, Huber R |
| Title | Investigations on the maturation and regulation of archaebacterial proteasomes. |
| Related PDB | |
| Related UniProtKB | |
| [27] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15916965 |
| Journal | Mol Cell |
| Year | 2005 |
| Volume | 18 |
| Pages | 589-99 |
| Authors | Forster A, Masters EI, Whitby FG, Robinson H, Hill CP |
| Title | The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions. |
| Related PDB | 1ya7 1yar 1yau |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme was transferred from E.C. The structure of this enzyme is cylindrical with four layers of seven subunits, According to the literature [18], (1) Alpha-amino group of Thr1 acts as a general base to activate the nucleophile, (2) Thr1 makes a nucleophilic attack on the carbonyl carbon of the target peptide bond, (3) The alpha-amino group of Thr1 acts as a general acid to protonate the leaving group, (4) Alpha-amino group of Thr1 acts as a general base to activate the NUK water, ### Autocatalysis, |
| Created | Updated |
|---|---|
| 2002-07-01 | 2010-02-03 |