DB code: S00296

RLCP classification 1.13.30000.12 : Hydrolysis
CATH domain 3.40.50.200 : Rossmann fold Catalytic domain
E.C. 3.4.21.100
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.200 : Rossmann fold S00295 D00219 S00519

Uniprot Enzyme Name
UniprotKB Protein name Synonyms MEROPS Pfam
P42790 Pseudomonalisin
EC 3.4.21.100
Pepstatin-insensitive carboxyl proteinase
Pseudomonapepsin
S53.001 (Serine)
PF00082 (Peptidase_S8)
PF09286 (Pro-kuma_activ)
[Graphical View]

KEGG enzyme name
sedolisin
Pseudomonas sp. pepstatin-insensitive carboxyl proteinase
pseudomonapepsin
pseudomonalisin
sedolysin

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P42790 PICP_PSESR Hydrolysis 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. Periplasm. Binds 1 calcium ion per subunit.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00017 C00001 C00012 I00087 I00085 I00086
E.C.
Compound Protein H2O Peptide Peptidyl-tetrahedral intermediate Acyl-enzyme Tetrahedral intermediate
Type peptide/protein H2O peptide/protein
ChEBI 15377
PubChem 22247451
962
1ga1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:UNK-PHI-UNK Unbound Unbound Unbound
1ga4A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Intermediate-bound:IVA-PHI-TYB Unbound
1ga6A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1kdvA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Intermediate-bound:ACE-ILE-ALA-PHA Unbound
1kdyA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Intermediate-bound:ACE-ILE-PRO-PHA Unbound
1kdzA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Transition-state-analogue:IVA-TYR-LEU-TYB
1ke1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Transition-state-analogue:IVA-TYR-TYB
1ke2A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Transition-state-analogue:CSI-LEU-PHA

Reference for Active-site residues
resource references E.C.
Swiss-prot & literature [1],[3]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ga1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 80;ASP 84;ASP 170;SER 287 SER 287
1ga4A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 80;ASP 84;ASP 170;SER 287 SER 287
1ga6A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 80;ASP 84;ASP 170;SER 287 SER 287
1kdvA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 80;ASP 84;ASP 170;SER 287 SER 287
1kdyA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 80;ASP 84;ASP 170;SER 287 SER 287
1kdzA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 80;ASP 84;ASP 170;SER 287 SER 287
1ke1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 80;ASP 84;ASP 170;SER 287 SER 287
1ke2A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 80;ASP 84;ASP 170;SER 287 SER 287

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
p.445-446
[4]
p.15609
[5]
p.88-92

References
[1]
Resource
Comments active site (mutation analysis)
Medline ID 99419069
PubMed ID 10488127
Journal J Biol Chem
Year 1999
Volume 274
Pages 27815-22
Authors Hiroshi Oyama, Shin-ichiro Abe, Souko Ushiyama, Saori Takahashi, and Kohei Oda
Title Identification of Catalytic Residues of Pepstatin-insensitive Carboxyl Proteinases from Prokaryotes by Site-directed Mutagenesis
Related PDB 1ga6
Related UniProtKB P42790
[2]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11173470
Journal Acta Crystallogr D
Year 2001
Volume 57
Pages 239-49
Authors Dauter Z, Li M, Wlodawer A
Title Practical experience with the use of halides for phasing macromolecular structures: a powerful tool for structural genomics.
Related PDB 1ga1
Related UniProtKB
[3]
Resource
Comments X-ray crystallography (1.0-1.4 Angstroms)
Medline ID
PubMed ID 11323721
Journal Nat Struct Biol
Year 2001
Volume 8
Pages 442-6
Authors Wlodawer A, Li M, Dauter Z, Gustchina A, Uchida K, Oyama H, Dunn BM, Oda K
Title Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes.
Related PDB 1ga4 1ga6
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 11747435
Journal Biochemistry
Year 2001
Volume 40
Pages 15602-11
Authors Wlodawer A, Li M, Gustchina A, Dauter Z, Uchida K, Oyama H, Goldfarb NE, Dunn BM, Oda K
Title Inhibitor complexes of the Pseudomonas serine-carboxyl proteinase.
Related PDB 1kdv 1kdy 1kdz 1ke1 1ke2
Related UniProtKB
[5]
Resource
Comments Review
Medline ID
PubMed ID 12673349
Journal Acta Biochim Pol
Year 2003
Volume 50
Pages 81-102
Authors Wlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K
Title Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases.
Related PDB
Related UniProtKB

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]).

Created Updated
2002-07-04 2011-02-22