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
PubChem 22247451
962
1hpgA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hpgA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1hpgA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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, GluSGP, and protease V8.
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, synthesis, and application.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to the peptidase family-S1E.
This enzyme has got a classical catalytic triad, composed of Ser/His/Asp, suggesting that it has a similar catalytic mechanism to that of trypsin (D00197 in EzCatDB).

Created Updated
2004-10-29 2011-02-21