DB code: D00185

CATH domain 3.40.350.10 : Creatine Amidinohydrolase; Chain A, domain 1
3.90.230.10 : Creatine Amidinohydrolase Catalytic domain
E.C. 3.4.11.9
CSA 1a16
M-CSA 1a16
MACiE

CATH domain Related DB codes (homologues)
3.40.350.10 : Creatine Amidinohydrolase; Chain A, domain 1 D00244
3.90.230.10 : Creatine Amidinohydrolase D00244

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq MEROPS Pfam
P15034 Xaa-Pro aminopeptidase
EC 3.4.11.9
X-Pro aminopeptidase
Aminopeptidase P II
APP-II
Aminoacylproline aminopeptidase
NP_417384.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491109.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
M24.004 (Metallo)
PF05195 (AMP_N)
PF00557 (Peptidase_M24)
[Graphical View]

KEGG enzyme name
Xaa-Pro aminopeptidase
proline aminopeptidase
aminopeptidase P
aminoacylproline aminopeptidase
X-Pro aminopeptidase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P15034 AMPP_ECOLI Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Homotetramer. Cytoplasm. Binds 2 manganese ions per subunit.

KEGG Pathways
Map code Pathways E.C.

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00034 C00012 C00001 C00045 C02186
E.C.
Compound Manganese Peptide H2O Amino acid Prolyl-peptide
Type heavy metal peptide/protein H2O amino acids amide group,amine group,carboxyl group
ChEBI 18291
35154
15377
PubChem 23930
22247451
962
1a16A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1az9A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1jawA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1m35A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1m35B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1m35C01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1m35D01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1m35E01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1m35F01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1a16A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:2x_MN Unbound Unbound Bound:PRO-LEU (chain L)
1az9A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:2x_MN Unbound Unbound Unbound
1jawA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:2x_MN Unbound Unbound Unbound
1m35A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:2x_MN Unbound Unbound Unbound
1m35B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:2x_MN Unbound Unbound Unbound
1m35C02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:2x_MN Unbound Unbound Unbound
1m35D02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:2x_MN Unbound Unbound Unbound
1m35E02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:2x_MN Unbound Unbound Unbound
1m35F02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:2x_MN Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot & literature [5]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1a16A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1az9A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jawA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1m35A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1m35B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1m35C01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1m35D01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1m35E01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1m35F01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1a16A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 383 ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)
1az9A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 383 ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)
1jawA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 383 ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)
1m35A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 383 ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)
1m35B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 383 ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)
1m35C02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 383 ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)
1m35D02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 383 ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)
1m35E02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 383 ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)
1m35F02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 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
References Sections No. of steps in catalysis
[5]
Fig.3 2
[6]
Fig.7, p.14817-14818 3
[8]
p.15134-15135

References
[1]
Resource
Comments
Medline ID
PubMed ID 4318
Journal Eur J Biochem
Year 1976
Volume 63
Pages 271-87
Authors Kessler E, Yaron A
Title An extracellular aminopeptidase from Clostridium histolyticum.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 7397119
Journal Biochemistry
Year 1980
Volume 19
Pages 3055-9
Authors Lin LN, Brandts JF
Title Kinetic mechanism for conformational transitions between poly-L-prolines I and II: a study utilizing the cis-trans specificity of a proline-specific protease.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 6441592
Journal Biochemistry
Year 1984
Volume 23
Pages 5713-23
Authors Lin LN, Brandts JF
Title Involvement of prolines-114 and -117 in the slow refolding phase of ribonuclease A as determined by isomer-specific proteolysis.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 8146141
Journal Proc Natl Acad Sci U S A
Year 1994
Volume 91
Pages 2473-7
Authors Bazan JF, Weaver LH, Roderick SL, Huber R, Matthews BW
Title Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold.
Related PDB
Related UniProtKB
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID 98188227
PubMed ID 9520390
Journal Proc Natl Acad Sci U S A
Year 1998
Volume 95
Pages 3472-7
Authors Wilce MC, Bond CS, Dixon NE, Freeman HC, Guss JM, Lilley PE, Wilce JA
Title Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli.
Related PDB 1a16 1az9 1jaw
Related UniProtKB P15034
[6]
Resource
Comments
Medline ID
PubMed ID 10555963
Journal Biochemistry
Year 1999
Volume 38
Pages 14810-9
Authors Lowther WT, Zhang Y, Sampson PB, Honek JF, Matthews BW
Title Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 10395480
Journal J Med Chem
Year 1999
Volume 42
Pages 2394-402
Authors Maggiora LL, Orawski AT, Simmons WH
Title Apstatin analogue inhibitors of aminopeptidase P, a bradykinin-degrading enzyme.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 11106491
Journal Biochemistry
Year 2000
Volume 39
Pages 15129-35
Authors Cottrell GS, Hyde RJ, Lim J, Parsons MR, Hooper NM, Turner AJ
Title Identification of critical residues in the active site of porcine membrane-bound aminopeptidase P.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 11516173
Journal Arch Biochem Biophys
Year 2001
Volume 393
Pages 163-9
Authors Iwase A, Nomura S, Mizutani S
Title Characterization of a secretase activity for placental leucine aminopeptidase.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 11423553
Journal J Biol Chem
Year 2001
Volume 276
Pages 31732-7
Authors Hauser F, Strassner J, Schaller A
Title Cloning, expression, and characterization of tomato (Lycopersicon esculentum) aminopeptidase P.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 11872174
Journal J Biochem (Tokyo)
Year 2002
Volume 131
Pages 445-52
Authors Kulkarni GV, Deobagkar DD
Title A cytosolic form of aminopeptidase P from Drosophila melanogaster: molecular cloning and characterization.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-03-25 2009-02-26