EzCatDB: D00185

DB codeD00185
CATH domainDomain 13.40.350.10
Domain 23.90.230.10Catalytic domain
E.C.3.4.11.9
CSA1a16

CATH domainRelated DB codes (homologues)
3.40.350.10D00244
3.90.230.10D00244

Enzyme Name
Swiss-protKEGG

P15034
Protein nameXaa-Pro aminopeptidaseXaa-Pro aminopeptidase
proline aminopeptidase
aminopeptidase P
aminoacylproline aminopeptidase
X-Pro aminopeptidase
SynonymsEC 3.4.11.9
X-Pro aminopeptidase
Aminopeptidase P II
APP-II
Aminoacylproline aminopeptidase


Swiss-prot:Accession NumberP15034
Entry nameAMPP_ECOLI
ActivityRelease of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.
SubunitHomotetramer.
Subcellular locationCytoplasm.
CofactorBinds 2 manganese ions per subunit.


CofactorsSubstratesProducts
KEGG-idC00034C00012C00001C00045C02186
CompoundManganesePeptideH2OAmino acidProlyl-peptide
Typeheavy metalpeptide/proteinH2Oamino acidsamide group,amine group,carboxyl group
1a16A01UnboundUnbound
UnboundUnbound
1az9A01UnboundUnbound
UnboundUnbound
1jawA01UnboundUnbound
UnboundUnbound
1m35A01UnboundUnbound
UnboundUnbound
1m35B01UnboundUnbound
UnboundUnbound
1m35C01UnboundUnbound
UnboundUnbound
1m35D01UnboundUnbound
UnboundUnbound
1m35E01UnboundUnbound
UnboundUnbound
1m35F01UnboundUnbound
UnboundUnbound
1a16A02Bound:2x_MNUnbound
UnboundBound:PRO-LEU(chain L)
1az9A02Bound:2x_MNUnbound
UnboundUnbound
1jawA02Bound:2x_MNUnbound
UnboundUnbound
1m35A02Bound:2x_MNUnbound
UnboundUnbound
1m35B02Bound:2x_MNUnbound
UnboundUnbound
1m35C02Bound:2x_MNUnbound
UnboundUnbound
1m35D02Bound:2x_MNUnbound
UnboundUnbound
1m35E02Bound:2x_MNUnbound
UnboundUnbound
1m35F02Bound:2x_MNUnbound
UnboundUnbound

Active-site residues
resource
Swiss-prot & literature [5]
pdbCatalytic residuesCofactor-binding residues
1a16A01

1az9A01

1jawA01

1m35A01

1m35B01

1m35C01

1m35D01

1m35E01

1m35F01

1a16A02GLU 383
ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)
1az9A02GLU 383
ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)
1jawA02GLU 383
ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)
1m35A02GLU 383
ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)
1m35B02GLU 383
ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)
1m35C02GLU 383
ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)
1m35D02GLU 383
ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)
1m35E02GLU 383
ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)
1m35F02GLU 383
ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[5]Fig.32
[6]Fig.7, p.14817-148183
[8]p.15134-15135

references
[1]
PubMed ID4318
JournalEur J Biochem
Year1976
Volume63
Pages271-87
AuthorsKessler E, Yaron A
TitleAn extracellular aminopeptidase from Clostridium histolyticum.
[2]
PubMed ID7397119
JournalBiochemistry
Year1980
Volume19
Pages3055-9
AuthorsLin LN, Brandts JF
TitleKinetic mechanism for conformational transitions between poly-L-prolines I and II: a study utilizing the cis-trans specificity of a proline-specific protease.
[3]
PubMed ID6441592
JournalBiochemistry
Year1984
Volume23
Pages5713-23
AuthorsLin LN, Brandts JF
TitleInvolvement of prolines-114 and -117 in the slow refolding phase of ribonuclease A as determined by isomer-specific proteolysis.
[4]
PubMed ID8146141
JournalProc Natl Acad Sci U S A
Year1994
Volume91
Pages2473-7
AuthorsBazan JF, Weaver LH, Roderick SL, Huber R, Matthews BW
TitleSequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID98188227
PubMed ID9520390
JournalProc Natl Acad Sci U S A
Year1998
Volume95
Pages3472-7
AuthorsWilce MC, Bond CS, Dixon NE, Freeman HC, Guss JM, Lilley PE, Wilce JA
TitleStructure and mechanism of a proline-specific aminopeptidase from Escherichia coli.
Related PDB1a16,1az9,1jaw
Related Swiss-protP15034
[6]
PubMed ID10555963
JournalBiochemistry
Year1999
Volume38
Pages14810-9
AuthorsLowther WT, Zhang Y, Sampson PB, Honek JF, Matthews BW
TitleInsights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues.
[7]
PubMed ID10395480
JournalJ Med Chem
Year1999
Volume42
Pages2394-402
AuthorsMaggiora LL, Orawski AT, Simmons WH
TitleApstatin analogue inhibitors of aminopeptidase P, a bradykinin-degrading enzyme.
[8]
PubMed ID11106491
JournalBiochemistry
Year2000
Volume39
Pages15129-35
AuthorsCottrell GS, Hyde RJ, Lim J, Parsons MR, Hooper NM, Turner AJ
TitleIdentification of critical residues in the active site of porcine membrane-bound aminopeptidase P.
[9]
PubMed ID11516173
JournalArch Biochem Biophys
Year2001
Volume393
Pages163-9
AuthorsIwase A, Nomura S, Mizutani S
TitleCharacterization of a secretase activity for placental leucine aminopeptidase.
[10]
PubMed ID11423553
JournalJ Biol Chem
Year2001
Volume276
Pages31732-7
AuthorsHauser F, Strassner J, Schaller A
TitleCloning, expression, and characterization of tomato (Lycopersicon esculentum) aminopeptidase P.
[11]
PubMed ID11872174
JournalJ Biochem (Tokyo)
Year2002
Volume131
Pages445-52
AuthorsKulkarni GV, Deobagkar DD
TitleA cytosolic form of aminopeptidase P from Drosophila melanogaster: molecular cloning and characterization.


createdupdated
2004-03-252009-02-26


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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