EzCatDB: S00296
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DB codeS00296
RLCP classification1.13.30000.12 : Hydrolysis
CATH domainDomain 13.40.50.200 : Rossmann foldCatalytic domain
E.C.3.4.21.100

CATH domainRelated DB codes (homologues)
3.40.50.200 : Rossmann foldS00295,D00219,S00519

Enzyme Name
UniProtKBKEGG

P42790
Protein namePseudomonalisinsedolisin
Pseudomonas sp. pepstatin-insensitive carboxyl proteinase
pseudomonapepsin
pseudomonalisin
sedolysin
SynonymsEC 3.4.21.100
Pepstatin-insensitive carboxyl proteinase
Pseudomonapepsin
MEROPSS53.001 (Serine)
PfamPF00082 (Peptidase_S8)
PF09286 (Pro-kuma_activ)
[Graphical view]


UniProtKB:Accession NumberP42790
Entry namePICP_PSESR
ActivityHydrolysis of the B chain of insulin at 13- Glu-|-Ala-14, 15-Leu-|-Tyr-16 and 25-Phe-|-Tyr-26 and angiotensin I at 4-Tyr-|-Ile-5. A good synthetic substrate is Lys-Pro-Ile-Glu- Phe-|-Phe(NO(2))-Arg-Leu.
Subunit
Subcellular locationPeriplasm.
CofactorBinds 1 calcium ion per subunit.

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00017C00001C00012I00087I00085I00086
CompoundProteinH2OPeptidePeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typepeptide/proteinH2Opeptide/protein


ChEBI
15377




PubChem
22247451
962




              
1ga1AUnbound Bound:UNK-PHI-UNKUnboundUnboundUnbound
1ga4AUnbound UnboundUnboundIntermediate-bound:IVA-PHI-TYBUnbound
1ga6AUnbound UnboundUnboundUnboundUnbound
1kdvAUnbound UnboundUnboundIntermediate-bound:ACE-ILE-ALA-PHAUnbound
1kdyAUnbound UnboundUnboundIntermediate-bound:ACE-ILE-PRO-PHAUnbound
1kdzAUnbound UnboundUnboundUnboundTransition-state-analogue:IVA-TYR-LEU-TYB
1ke1AUnbound UnboundUnboundUnboundTransition-state-analogue:IVA-TYR-TYB
1ke2AUnbound UnboundUnboundUnboundTransition-state-analogue:CSI-LEU-PHA

Active-site residues
resource
Swiss-prot & literature [1],[3]
pdbCatalytic residuesMain-chain involved in catalysis
          
1ga1AGLU 80;ASP 84;ASP 170;SER 287
SER 287
1ga4AGLU 80;ASP 84;ASP 170;SER 287
SER 287
1ga6AGLU 80;ASP 84;ASP 170;SER 287
SER 287
1kdvAGLU 80;ASP 84;ASP 170;SER 287
SER 287
1kdyAGLU 80;ASP 84;ASP 170;SER 287
SER 287
1kdzAGLU 80;ASP 84;ASP 170;SER 287
SER 287
1ke1AGLU 80;ASP 84;ASP 170;SER 287
SER 287
1ke2AGLU 80;ASP 84;ASP 170;SER 287
SER 287

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.445-446
[4]p.15609
[5]p.88-92

references
[1]
Commentsactive site (mutation analysis)
Medline ID99419069
PubMed ID10488127
JournalJ Biol Chem
Year1999
Volume274
Pages27815-22
AuthorsHiroshi Oyama, Shin-ichiro Abe, Souko Ushiyama, Saori Takahashi, and Kohei Oda
TitleIdentification of Catalytic Residues of Pepstatin-insensitive Carboxyl Proteinases from Prokaryotes by Site-directed Mutagenesis
Related PDB1ga6
Related UniProtKBP42790
[2]
CommentsX-ray crystallography
PubMed ID11173470
JournalActa Crystallogr D
Year2001
Volume57
Pages239-49
AuthorsDauter Z, Li M, Wlodawer A
TitlePractical experience with the use of halides for phasing macromolecular structures: a powerful tool for structural genomics.
Related PDB1ga1
[3]
CommentsX-ray crystallography (1.0-1.4 Angstroms)
PubMed ID11323721
JournalNat Struct Biol
Year2001
Volume8
Pages442-6
AuthorsWlodawer A, Li M, Dauter Z, Gustchina A, Uchida K, Oyama H, Dunn BM, Oda K
TitleCarboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes.
Related PDB1ga4,1ga6
[4]
PubMed ID11747435
JournalBiochemistry
Year2001
Volume40
Pages15602-11
AuthorsWlodawer A, Li M, Gustchina A, Dauter Z, Uchida K, Oyama H, Goldfarb NE, Dunn BM, Oda K
TitleInhibitor complexes of the Pseudomonas serine-carboxyl proteinase.
Related PDB1kdv,1kdy,1kdz,1ke1,1ke2
[5]
CommentsReview
PubMed ID12673349
JournalActa Biochim Pol
Year2003
Volume50
Pages81-102
AuthorsWlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K
TitleStructural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases.

comments
According to the papers [3], [4] & [5], Ser287 and the acidic residues seem to comprise the catalytic residues, although the detailed catalytic mechanism remains still unknown. However, the catalytic serine residue plays a role as nucleophile, which will attack the carbonyl carbon atom and make a covalent bond with the atom (see [3], [4] & [5]). The paper [3] suggested that Glu80 might be a general base that will abstract the proton of the -OH group of the catalytic serine. Thus, Ser287-Glu80-Asp84 constitute the catalytic triad, whilst Asp170 seems to be a part of oxyanion hole stabilizing the tetrahedral intermediate of the reaction (see [3] & [4]).

createdupdated
2002-07-042011-02-22
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
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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