D00185
type: Enzyme
cath: Creatine Amidinohydrolase; Chain A, domain 1
cath: Creatine Amidinohydrolase
ec: https://purl.uniprot.org/enzyme/3.4.11.9
csa: 1a16
uniprot: P15034
kegg enzyme: Xaa-Pro aminopeptidase
kegg enzyme: proline aminopeptidase
kegg enzyme: aminopeptidase P
kegg enzyme: aminoacylproline aminopeptidase
kegg enzyme: X-Pro aminopeptidase
kegg cofactor: Manganese
kegg substrate: Peptide
kegg substrate: H2O
kegg product: Amino acid
kegg product: Prolyl-peptide
pdb: 1a16A01
pdb: 1az9A01
pdb: 1jawA01
pdb: 1m35A01
pdb: 1m35B01
pdb: 1m35C01
pdb: 1m35D01
pdb: 1m35E01
pdb: 1m35F01
pdb: 1a16A02
pdb: 1az9A02
pdb: 1jawA02
pdb: 1m35A02
pdb: 1m35B02
pdb: 1m35C02
pdb: 1m35D02
pdb: 1m35E02
pdb: 1m35F02
pdb bound state: Unbound
  compound: Peptide
  pdb: 1a16A01
pdb bound state: Unbound
  compound: Peptide
  pdb: 1az9A01
pdb bound state: Unbound
  compound: Peptide
  pdb: 1jawA01
pdb bound state: Unbound
  compound: Peptide
  pdb: 1m35A01
pdb bound state: Unbound
  compound: Peptide
  pdb: 1m35B01
pdb bound state: Unbound
  compound: Peptide
  pdb: 1m35C01
pdb bound state: Unbound
  compound: Peptide
  pdb: 1m35D01
pdb bound state: Unbound
  compound: Peptide
  pdb: 1m35E01
pdb bound state: Unbound
  compound: Peptide
  pdb: 1m35F01
pdb bound state: Unbound
  compound: Peptide
  pdb: 1a16A02
pdb bound state: Unbound
  compound: Peptide
  pdb: 1az9A02
pdb bound state: Unbound
  compound: Peptide
  pdb: 1jawA02
pdb bound state: Unbound
  compound: Peptide
  pdb: 1m35A02
pdb bound state: Unbound
  compound: Peptide
  pdb: 1m35B02
pdb bound state: Unbound
  compound: Peptide
  pdb: 1m35C02
pdb bound state: Unbound
  compound: Peptide
  pdb: 1m35D02
pdb bound state: Unbound
  compound: Peptide
  pdb: 1m35E02
pdb bound state: Unbound
  compound: Peptide
  pdb: 1m35F02
pdb bound state: Unbound
  compound: Manganese
  pdb: 1a16A01
pdb bound state: Unbound
  compound: Manganese
  pdb: 1az9A01
pdb bound state: Unbound
  compound: Manganese
  pdb: 1jawA01
pdb bound state: Unbound
  compound: Manganese
  pdb: 1m35A01
pdb bound state: Unbound
  compound: Manganese
  pdb: 1m35B01
pdb bound state: Unbound
  compound: Manganese
  pdb: 1m35C01
pdb bound state: Unbound
  compound: Manganese
  pdb: 1m35D01
pdb bound state: Unbound
  compound: Manganese
  pdb: 1m35E01
pdb bound state: Unbound
  compound: Manganese
  pdb: 1m35F01
pdb bound state: Unbound
  compound: Amino acid
  pdb: 1a16A01
pdb bound state: Unbound
  compound: Amino acid
  pdb: 1az9A01
pdb bound state: Unbound
  compound: Amino acid
  pdb: 1jawA01
pdb bound state: Unbound
  compound: Amino acid
  pdb: 1m35A01
pdb bound state: Unbound
  compound: Amino acid
  pdb: 1m35B01
pdb bound state: Unbound
  compound: Amino acid
  pdb: 1m35C01
pdb bound state: Unbound
  compound: Amino acid
  pdb: 1m35D01
active site residues resources: Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues.
references: An extracellular aminopeptidase from Clostridium histolyticum.
references: Kinetic mechanism for conformational transitions between poly-L-prolines I and II: a study utilizing the cis-trans specificity of a proline-specific protease.
references: Involvement of prolines-114 and -117 in the slow refolding phase of ribonuclease A as determined by isomer-specific proteolysis.
references: Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold.
references: Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli.
references: Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues.
references: Apstatin analogue inhibitors of aminopeptidase P, a bradykinin-degrading enzyme.
references: Identification of critical residues in the active site of porcine membrane-bound aminopeptidase P.
references: Characterization of a secretase activity for placental leucine aminopeptidase.
references: Cloning, expression, and characterization of tomato (Lycopersicon esculentum) aminopeptidase P.
references: A cytosolic form of aminopeptidase P from Drosophila melanogaster: molecular cloning and characterization.

Creatine Amidinohydrolase; Chain A, domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.350.10

Creatine Amidinohydrolase
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.90.230.10
catalytic domain: index.html

Manganese
type: KeggCofactor
references: KEGG:C00034
compound type: heavy metal
references: CHEBI:18291
references: CHEBI:35154
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Peptide
type: KeggSubstrate
references: KEGG:C00012
compound type: peptide/protein

H2O
type: KeggSubstrate
references: KEGG:C00001
compound type: H2O
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Amino acid
type: KeggProduct
references: KEGG:C00045
compound type: amino acids

Prolyl-peptide
type: KeggProduct
references: KEGG:C02186
compound type: amide group
compound type: amine group
compound type: carboxyl group

1a16A02
type: Pdb
references: 1a16
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a16
catalytic residue: GLU 383
cofactor binding residue: ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)

1az9A02
type: Pdb
references: 1az9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1az9
catalytic residue: GLU 383
cofactor binding residue: ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)

1jawA02
type: Pdb
references: 1jaw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jaw
catalytic residue: GLU 383
cofactor binding residue: ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)

1m35A02
type: Pdb
references: 1m35
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1m35
catalytic residue: GLU 383
cofactor binding residue: ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)

1m35B02
type: Pdb
references: 1m35
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1m35
catalytic residue: GLU 383
cofactor binding residue: ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)

1m35C02
type: Pdb
references: 1m35
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1m35
catalytic residue: GLU 383
cofactor binding residue: ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)

1m35D02
type: Pdb
references: 1m35
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1m35
catalytic residue: GLU 383
cofactor binding residue: ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)

1m35E02
type: Pdb
references: 1m35
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1m35
catalytic residue: GLU 383
cofactor binding residue: ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)

1m35F02
type: Pdb
references: 1m35
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1m35
catalytic residue: GLU 383
cofactor binding residue: ASP 260(Manganese-2 binding);HIS 354;GLU 383(Manganese-1 binding);ASP 271;GLU 406(Manganese-1 & -2 binding)

An extracellular aminopeptidase from Clostridium histolyticum.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/4318
journal: Eur J Biochem
volume: 63
pages: 271-87
published year: 1976
authors:
  item: Kessler E
  item: Yaron A

Kinetic mechanism for conformational transitions between poly-L-prolines I and II: a study utilizing the cis-trans specificity of a proline-specific protease.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7397119
journal: Biochemistry
volume: 19
pages: 3055-9
published year: 1980
authors:
  item: Lin LN
  item: Brandts JF

Involvement of prolines-114 and -117 in the slow refolding phase of ribonuclease A as determined by isomer-specific proteolysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6441592
journal: Biochemistry
volume: 23
pages: 5713-23
published year: 1984
authors:
  item: Lin LN
  item: Brandts JF

Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8146141
journal: Proc Natl Acad Sci U S A
volume: 91
pages: 2473-7
published year: 1994
authors:
  item: Bazan JF
  item: Weaver LH
  item: Roderick SL
  item: Huber R
  item: Matthews BW

Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
medline id: 98188227
references: http://www.ncbi.nlm.nih.gov/pubmed/9520390
journal: Proc Natl Acad Sci U S A
volume: 95
pages: 3472-7
published year: 1998
authors:
  item: Wilce MC
  item: Bond CS
  item: Dixon NE
  item: Freeman HC
  item: Guss JM
  item: Lilley PE
  item: Wilce JA
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P15034

Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10555963
journal: Biochemistry
volume: 38
pages: 14810-9
published year: 1999
authors:
  item: Lowther WT
  item: Zhang Y
  item: Sampson PB
  item: Honek JF
  item: Matthews BW

Apstatin analogue inhibitors of aminopeptidase P, a bradykinin-degrading enzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10395480
journal: J Med Chem
volume: 42
pages: 2394-402
published year: 1999
authors:
  item: Maggiora LL
  item: Orawski AT
  item: Simmons WH

Identification of critical residues in the active site of porcine membrane-bound aminopeptidase P.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11106491
journal: Biochemistry
volume: 39
pages: 15129-35
published year: 2000
authors:
  item: Cottrell GS
  item: Hyde RJ
  item: Lim J
  item: Parsons MR
  item: Hooper NM
  item: Turner AJ

Characterization of a secretase activity for placental leucine aminopeptidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11516173
journal: Arch Biochem Biophys
volume: 393
pages: 163-9
published year: 2001
authors:
  item: Iwase A
  item: Nomura S
  item: Mizutani S

Cloning, expression, and characterization of tomato (Lycopersicon esculentum) aminopeptidase P.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11423553
journal: J Biol Chem
volume: 276
pages: 31732-7
published year: 2001
authors:
  item: Hauser F
  item: Strassner J
  item: Schaller A

A cytosolic form of aminopeptidase P from Drosophila melanogaster: molecular cloning and characterization.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11872174
journal: J Biochem (Tokyo)
volume: 131
pages: 445-52
published year: 2002
authors:
  item: Kulkarni GV
  item: Deobagkar DD

ReferenceForCatalyticMechanism
reference index: 5
reference section: Fig.3
reference step: 2

ReferenceForCatalyticMechanism
reference index: 6
reference section: Fig.7, p.14817-14818
reference step: 3

ReferenceForCatalyticMechanism
reference index: 8
reference section: p.15134-15135