DB code: S00353

RLCP classification 1.13.30000.10 : Hydrolysis
CATH domain 3.40.50.1820 : Rossmann fold Catalytic domain
E.C. 3.4.11.5
CSA 1azw
M-CSA 1azw
MACiE

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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms MEROPS Pfam
P52279 Proline iminopeptidase
PIP
EC 3.4.11.5
Prolyl aminopeptidase
PAP
S33.001 (Serine)
PF00561 (Abhydrolase_1)
[Graphical View]
O32449 Proline iminopeptidase
PIP
EC 3.4.11.5
Prolyl aminopeptidase
PAP
S33.001 (Serine)
PF00561 (Abhydrolase_1)
[Graphical View]

KEGG enzyme name
prolyl aminopeptidase
proline aminopeptidase
Pro-X aminopeptidase
cytosol aminopeptidase V
proline iminopeptidase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P52279 PIP_XANCI Release of N-terminal proline from a peptide. Homooligomer. Cytoplasm (By similarity).
O32449 PIP_SERMA Release of N-terminal proline from a peptide. Monomer. Cytoplasm.

KEGG Pathways
Map code Pathways E.C.
MAP00330 Arginine and proline metabolism
MAP00480 Glutathione metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00034 C00012 C00001 C01843 C03305 C00148 C00012 I00087 I00085 I00086
E.C.
Compound Manganese,Mn2+ Peptide H2O Polyproline Prolyl-2-naphthylamide L-Proline Peptide Peptidyl-tetrahedral intermediate Acyl-enzyme Tetrahedral intermediate
Type heavy metal peptide/protein H2O peptide/protein amide group,amine group,aromatic ring (only carbon atom) amino acids peptide/protein
ChEBI 18291
35154
15377
73647
17203
60039
PubChem 23930
22247451
962
11877119
439587
439971
145742
6971047
1azwA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1azwB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1qtrA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1azwA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 110;ASP 266;HIS 294
1azwB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 110;ASP 266;HIS 294
1qtrA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 113;ASP 268;HIS 296

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
p.2-4
[4]
p.504
[5]
p.561-562, Fig.7
[7]
p.221

References
[1]
Resource
Comments
Medline ID
PubMed ID 1459939
Journal J Bacteriol
Year 1992
Volume 174
Pages 7919-25
Authors Kitazono A, Yoshimoto T, Tsuru D
Title Cloning, sequencing, and high expression of the proline iminopeptidase gene from Bacillus coagulans.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 9000519
Journal FEBS Lett
Year 1997
Volume 400
Pages 91-3
Authors Medrano FJ, Alonso J, Garcia JL, Bode W, Gomis-Ruth FX
Title Crystallization and preliminary X-ray diffraction analysis of proline iminopeptidase from Xanthomonas campestris pv. citri.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-ray crystallography (2.7 Angstroms)
Medline ID
PubMed ID 9427736
Journal EMBO J
Year 1998
Volume 17
Pages 1-9
Authors Medrano FJ, Alonso J, Garcia JL, Romero A, Bode W, Gomis-Ruth FX
Title Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family.
Related PDB 1azw
Related UniProtKB
[4]
Resource
Comments catalysis (mutation analysis)
Medline ID
PubMed ID 9989236
Journal Biochim Biophys Acta
Year 1999
Volume 1429
Pages 501-5
Authors Morel F, Gilbert C, Geourjon C, Frot-Coutaz J, Portalier R, Atlan D
Title The prolyl aminopeptidase from Lactobacillus delbrueckii subsp. bulgaricus belongs to the alpha/beta hydrolase fold family.
Related PDB
Related UniProtKB
[5]
Resource
Comments X-ray crystallography (2.3 Angstroms)
Medline ID
PubMed ID 10467172
Journal J Biochem (Tokyo)
Year 1999
Volume 126
Pages 559-65
Authors Yoshimoto T, Kabashima T, Uchikawa K, Inoue T, Tanaka N, Nakamura KT, Tsuru M, Ito K
Title Crystal structure of prolyl aminopeptidase from Serratia marcescens.
Related PDB 1qtrA
Related UniProtKB
[6]
Resource
Comments catalysis
Medline ID
PubMed ID 11011150
Journal J Biochem (Tokyo)
Year 2000
Volume 128
Pages 673-8
Authors Ito K, Inoue T, Kabashima T, Kanada N, Huang HS, Ma X, Azmi N, Azab E, Yoshimoto T
Title Substrate recognition mechanism of prolyl aminopeptidase from Serratia marcescens.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 12369917
Journal Curr Protein Pept Sci
Year 2000
Volume 1
Pages 209-35
Authors Holmquist M
Title Alpha/Beta-hydrolase fold enzymes: structures, functions and mechanisms.
Related PDB
Related UniProtKB

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.

Created Updated
2002-07-01 2011-02-16