EzCatDB: D00435
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DB codeD00435
RLCP classification1.13.30000.10 : Hydrolysis
CATH domainDomain 12.40.10.10 : Thrombin, subunit HCatalytic domain
Domain 22.40.10.10 : Thrombin, subunit HCatalytic domain
E.C.3.4.21.82

CATH domainRelated DB codes (homologues)
2.40.10.10 : Thrombin, subunit HM00139,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

Enzyme Name
UniProtKBKEGG

Q07006
Protein nameGlutamyl endopeptidase 2glutamyl endopeptidase II
GluSGP
SynonymsEC 3.4.21.82
Glutamyl endopeptidase II
Glutamic acid-specific protease
GLUSGP
Streptogrisin-E
Serine protease E
SGPE
MEROPSS01.267 (Serine)
PfamPF00089 (Trypsin)
[Graphical view]


UniProtKB:Accession NumberQ07006
Entry nameGLUP_STRGR
ActivityPreferential 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.
SubunitMonomer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00012C00017C00001C00012C00017I00087I00085I00086
CompoundPeptideProteinH2OPeptideProteinPeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typepeptide/proteinpeptide/proteinH2Opeptide/proteinpeptide/protein


ChEBI

15377





PubChem

962
22247451





                
1hpgA01UnboundUnbound UnboundUnboundUnboundUnboundUnbound
1hpgA02UnboundUnbound Bound:BOC-ALA-ALA-PRO-GLU(chain B)UnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;Q07006
pdbCatalytic residuesMain-chain involved in catalysis
          
1hpgA01HIS 57;ASP 102
 
1hpgA02SER 195
GLY 193;SER 195


references
[1]
PubMed ID1794975
JournalJ Biochem (Tokyo)
Year1991
Volume110
Pages859-62
AuthorsNagata K, Yoshida N, Ogata F, Araki M, Noda K
TitleSubsite mapping of an acidic amino acid-specific endopeptidase from Streptomyces griseus, GluSGP, and protease V8.
[2]
PubMed ID1674942
JournalJ Biol Chem
Year1991
Volume266
Pages10727-30
AuthorsKomiyama T, Bigler TL, Yoshida N, Noda K, Laskowski M Jr
TitleReplacement 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).
[3]
CommentsX-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
Medline ID94032266
PubMed ID8105890
JournalBiochemistry
Year1993
Volume32
Pages11469-75
AuthorsNienaber VL, Breddam K, Birktoft JJ
TitleA glutamic acid specific serine protease utilizes a novel histidine triad in substrate binding.
Related PDB1hpg
Related UniProtKBQ07006
[4]
Comments3D-STRUCTURE MODELING.
Medline ID93279375
PubMed ID8504858
JournalFEBS Lett
Year1993
Volume324
Pages45-50
AuthorsBarbosa JA, Garratt RC, Saldanha JW
TitleA structural model for the glutamate-specific endopeptidase from Streptomyces griseus that explains substrate specificity.
Related UniProtKBQ07006
[5]
PubMed ID7925392
JournalEur J Biochem
Year1994
Volume224
Pages735-42
AuthorsKitadokoro K, Tsuzuki H, Okamoto H, Sato T
TitleCrystal structure analysis of a serine proteinase from Streptomyces fradiae at 0.16-nm resolution and molecular modeling of an acidic-amino-acid-specific proteinase.
[6]
PubMed ID11004534
JournalBiochim Biophys Acta
Year2000
Volume1479
Pages114-22
AuthorsWehofsky N, Wissmann J, Alisch M, Bordusa F
TitleEngineering of substrate mimetics as novel-type substrates for glutamic acid-specific endopeptidases: design, synthesis, and application.

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).

createdupdated
2004-10-292011-02-21


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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