EzCatDB: S00353

DB codeS00353
RLCP classification1.13.30000.10
CATH domainDomain 13.40.50.1820Catalytic domain
E.C.3.4.11.5
CSA1azw

CATH domainRelated DB codes (homologues)
3.40.50.1820S00544,S00344,S00517,S00525,S00526,S00720,S00723,S00724,S00725,S00919,S00057,S00374,S00345,S00347,S00348,S00346,S00350,S00352,S00355,S00356,S00358,D00189,D00210,D00539,T00253

Enzyme Name
Swiss-protKEGG

P52279O32449
Protein nameProline iminopeptidaseProline iminopeptidaseprolyl aminopeptidase
proline aminopeptidase
Pro-X aminopeptidase
cytosol aminopeptidase V
proline iminopeptidase
SynonymsPIP
EC 3.4.11.5
Prolyl aminopeptidase
PAP
PIP
EC 3.4.11.5
Prolyl aminopeptidase
PAP

KEGG pathways
MAP codePathways
MAP00330Arginine and proline metabolism
MAP00480Glutathione metabolism

Swiss-prot:Accession NumberP52279O32449
Entry namePIP_XANCIPIP_SERMA
ActivityRelease of N-terminal proline from a peptide.Release of N-terminal proline from a peptide.
SubunitHomooligomer.Monomer.
Subcellular locationCytoplasm (By similarity).Cytoplasm.
Cofactor



CofactorsSubstratesProductsintermediates
KEGG-idC00034C00012C00001C01843C03305C00148C00012I00087I00085I00086
CompoundManganese,Mn2+PeptideH2OPolyprolineProlyl-2-naphthylamideL-ProlinePeptidePeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typeheavy metalpeptide/proteinH2Opeptide/proteinamide group,amine group,aromatic ring (only carbon atom)amino acidspeptide/protein


1azwAUnboundUnbound
UnboundUnboundUnboundUnbound


1azwBUnboundUnbound
UnboundUnboundUnboundUnbound


1qtrAUnboundUnbound
UnboundUnboundUnboundUnbound



Active-site residues
resource
Swiss-prot
pdbCatalytic residues
1azwASER 110;ASP 266;HIS 294
1azwBSER 110;ASP 266;HIS 294
1qtrASER 113;ASP 268;HIS 296

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.2-4
[4]p.504
[5]p.561-562, Fig.7
[7]p.221

references
[1]
PubMed ID1459939
JournalJ Bacteriol
Year1992
Volume174
Pages7919-25
AuthorsKitazono A, Yoshimoto T, Tsuru D
TitleCloning, sequencing, and high expression of the proline iminopeptidase gene from Bacillus coagulans.
[2]
PubMed ID9000519
JournalFEBS Lett
Year1997
Volume400
Pages91-3
AuthorsMedrano FJ, Alonso J, Garcia JL, Bode W, Gomis-Ruth FX
TitleCrystallization and preliminary X-ray diffraction analysis of proline iminopeptidase from Xanthomonas campestris pv. citri.
[3]
CommentsX-ray crystallography (2.7 Angstroms)
PubMed ID9427736
JournalEMBO J
Year1998
Volume17
Pages1-9
AuthorsMedrano FJ, Alonso J, Garcia JL, Romero A, Bode W, Gomis-Ruth FX
TitleStructure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family.
Related PDB1azw
[4]
Commentscatalysis (mutation analysis)
PubMed ID9989236
JournalBiochim Biophys Acta
Year1999
Volume1429
Pages501-5
AuthorsMorel F, Gilbert C, Geourjon C, Frot-Coutaz J, Portalier R, Atlan D
TitleThe prolyl aminopeptidase from Lactobacillus delbrueckii subsp. bulgaricus belongs to the alpha/beta hydrolase fold family.
[5]
CommentsX-ray crystallography (2.3 Angstroms)
PubMed ID10467172
JournalJ Biochem (Tokyo)
Year1999
Volume126
Pages559-65
AuthorsYoshimoto T, Kabashima T, Uchikawa K, Inoue T, Tanaka N, Nakamura KT, Tsuru M, Ito K
TitleCrystal structure of prolyl aminopeptidase from Serratia marcescens.
Related PDB1qtrA
[6]
Commentscatalysis
PubMed ID11011150
JournalJ Biochem (Tokyo)
Year2000
Volume128
Pages673-8
AuthorsIto K, Inoue T, Kabashima T, Kanada N, Huang HS, Ma X, Azmi N, Azab E, Yoshimoto T
TitleSubstrate recognition mechanism of prolyl aminopeptidase from Serratia marcescens.
[7]
PubMed ID12369917
JournalCurr Protein Pept Sci
Year2000
Volume1
Pages209-35
AuthorsHolmquist M
TitleAlpha/Beta-hydrolase fold enzymes: structures, functions and mechanisms.

comments
This enzyme belongs to the peptidase family-S33.
Accoriding to the literature [3], [4], [5] & [7], this enzyme has got the catalytic triad, Ser110/His294/Asp266, along with "oxyanion hole" composed of mainchain atoms of Trp111 and Gly43.

createdupdated
2002-07-012011-02-16


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 2010)
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)

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