DB code: D00435
| RLCP classification | 1.13.30000.10 : Hydrolysis | |
|---|---|---|
| CATH domain | 2.40.10.10 : Thrombin, subunit H | Catalytic domain |
| 2.40.10.10 : Thrombin, subunit H | Catalytic domain | |
| E.C. | 3.4.21.82 | |
| CSA | ||
| M-CSA | ||
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 2.40.10.10 : Thrombin, subunit H | M00139 D00214 M00167 D00426 M00133 D00428 D00429 D00430 D00431 D00432 D00433 D00434 M00227 M00209 D00194 D00197 D00211 D00212 D00216 M00212 D00224 D00497 M00217 M00216 D00528 D00848 D00850 D00851 D00852 D00855 M00152 M00155 M00157 M00181 M00315 M00316 M00317 M00348 M00349 T00074 T00410 T00411 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | MEROPS | Pfam |
|---|---|---|---|---|
| Q07006 |
Glutamyl endopeptidase 2
|
EC
3.4.21.82
Glutamyl endopeptidase II Glutamic acid-specific protease GLUSGP Streptogrisin-E Serine protease E SGPE |
S01.267
(Serine)
|
PF00089
(Trypsin)
[Graphical View] |
| KEGG enzyme name |
|---|
|
glutamyl endopeptidase II
GluSGP |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| Q07006 | GLUP_STRGR | Preferential cleavage: -Glu-|-Xaa- >> -Asp-|- Xaa-. Preference for Pro or Leu at P2 and Phe at P3. Cleavage of -Glu-|-Asp- and -Glu-|-Pro- bonds is slow. | Monomer. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|
| Compound table | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Substrates | Products | Intermediates | |||||||||||
| KEGG-id | C00012 | C00017 | C00001 | C00012 | C00017 | I00087 | I00085 | I00086 | |||||
| E.C. | |||||||||||||
| Compound | Peptide | Protein | H2O | Peptide | Protein | Peptidyl-tetrahedral intermediate | Acyl-enzyme | Tetrahedral intermediate | |||||
| Type | peptide/protein | peptide/protein | H2O | peptide/protein | peptide/protein | ||||||||
| ChEBI |
15377 15377 |
||||||||||||
| PubChem |
22247451 962 22247451 962 |
||||||||||||
| 1hpgA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1hpgA02 |
|
|
|
|
|
Unbound | Unbound | Bound:BOC-ALA-ALA-PRO-GLU (chain B) | Unbound | Unbound | Unbound | Unbound | |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;Q07006 | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1hpgA01 |
|
|
|
|
|
HIS 57;ASP 102 | ||||
| 1hpgA02 |
|
|
|
|
|
SER 195 | GLY 193;SER 195 | |||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1794975 |
| Journal | J Biochem (Tokyo) |
| Year | 1991 |
| Volume | 110 |
| Pages | 859-62 |
| Authors | Nagata K, Yoshida N, Ogata F, Araki M, Noda K |
| Title |
Subsite mapping of an acidic amino acid-specific endopeptidase from Streptomyces griseus, |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1674942 |
| Journal | J Biol Chem |
| Year | 1991 |
| Volume | 266 |
| Pages | 10727-30 |
| Authors | Komiyama T, Bigler TL, Yoshida N, Noda K, Laskowski M Jr |
| Title | Replacement of P1 Leu18 by Glu18 in the reactive site of turkey ovomucoid third domain converts it into a strong inhibitor of Glu-specific Streptomyces griseus proteinase (GluSGP). |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS). |
| Medline ID | 94032266 |
| PubMed ID | 8105890 |
| Journal | Biochemistry |
| Year | 1993 |
| Volume | 32 |
| Pages | 11469-75 |
| Authors | Nienaber VL, Breddam K, Birktoft JJ |
| Title | A glutamic acid specific serine protease utilizes a novel histidine triad in substrate binding. |
| Related PDB | 1hpg |
| Related UniProtKB | Q07006 |
| [4] | |
| Resource | |
| Comments | 3D-STRUCTURE MODELING. |
| Medline ID | 93279375 |
| PubMed ID | 8504858 |
| Journal | FEBS Lett |
| Year | 1993 |
| Volume | 324 |
| Pages | 45-50 |
| Authors | Barbosa JA, Garratt RC, Saldanha JW |
| Title | A structural model for the glutamate-specific endopeptidase from Streptomyces griseus that explains substrate specificity. |
| Related PDB | |
| Related UniProtKB | Q07006 |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7925392 |
| Journal | Eur J Biochem |
| Year | 1994 |
| Volume | 224 |
| Pages | 735-42 |
| Authors | Kitadokoro K, Tsuzuki H, Okamoto H, Sato T |
| Title | Crystal structure analysis of a serine proteinase from Streptomyces fradiae at 0.16-nm resolution and molecular modeling of an acidic-amino-acid-specific proteinase. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11004534 |
| Journal | Biochim Biophys Acta |
| Year | 2000 |
| Volume | 1479 |
| Pages | 114-22 |
| Authors | Wehofsky N, Wissmann J, Alisch M, Bordusa F |
| Title |
Engineering of substrate mimetics as novel-type substrates for glutamic acid-specific endopeptidases: design, |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme belongs to the peptidase family-S1E.
This enzyme has got a classical catalytic triad, |
| Created | Updated |
|---|---|
| 2004-10-29 | 2011-02-21 |