M00101
type: Enzyme
cath: Collagenase (Catalytic Domain)
cath: Seminal Fluid Protein PDC-109 (Domain B)
cath: Hemopexin
ec: https://purl.uniprot.org/enzyme/3.4.24.24
csa: 1ck7
csa: 1qib
uniprot: P08253
kegg enzyme: gelatinase A
kegg enzyme: 72-kDa gelatinase
kegg enzyme: matrix metalloproteinase 2
kegg enzyme: type IV collagenase
kegg enzyme: 3/4 collagenase (Obsolete)
kegg enzyme: matrix metalloproteinase 5 (Obsolete)
kegg enzyme: 72 kDa gelatinase type A
kegg enzyme: collagenase IV
kegg enzyme: collagenase type IV
kegg enzyme: MMP 2
kegg enzyme: type IV collagen metalloproteinase
kegg enzyme: type IV collagenase/gelatinase
kegg cofactor: Zinc
kegg cofactor: Calcium
kegg substrate: Gelatin type I
kegg substrate: Collagen type IV
kegg substrate: Collagen type V
kegg substrate: Collagen type VII
kegg substrate: Collagen type X
kegg substrate: H2O
kegg product: Protein
kegg product: Peptide
pdb: 1ck7A01
pdb: 1qibA
pdb: 1gxdA01
pdb: 1gxdB01
pdb: 1eakA01
pdb: 1eakB01
pdb: 1eakC01
pdb: 1eakD01
pdb: 1ck7A02
pdb: 1gxdA02
pdb: 1gxdB02
pdb: 1eakA02
pdb: 1eakB02
pdb: 1eakC02
pdb: 1eakD02
pdb: 1ck7A03
pdb: 1gxdA03
pdb: 1gxdB03
pdb: 1eakA03
pdb: 1eakB03
pdb: 1eakC03
pdb: 1eakD03
pdb: 1cxwA
pdb: 1ck7A04
pdb: 1gxdA04
pdb: 1gxdB04
pdb: 1eakA04
pdb: 1eakB04
pdb: 1eakC04
pdb: 1eakD04
pdb: 1j7mA
pdb: 1ck7A05
pdb: 1gxdA05
pdb: 1gxdB05
references: Crystal structure of the haemopexin-like C-terminal domain of gelatinase A.
references: The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function.
references: X-ray structure of gelatinase a catalytic domain complexed with a hydroxamate inhibitor.
references: Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed.
references: The second type II module from human matrix metalloproteinase 2: structure, function and dynamics.
references: Gelatin-binding region of human matrix metalloproteinase-2: solution structure, dynamics, and function of the COL-23 two-domain construct.
references: Tyrosine 36 plays a critical role in the interaction of the AB loop of tissue inhibitor of metalloproteinases-2 with matrix metalloproteinase-14.
references: Specific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domain.
references: Substrate recognition by gelatinase A: the C-terminal domain facilitates surface diffusion.
references: Endostatin binds to the catalytic domain of matrix metalloproteinase-2.
references: Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2.
references: Solution structure and backbone dynamics of the catalytic domain of matrix metalloproteinase-2 complexed with a hydroxamic acid inhibitor.
references: Peptide ligands for the fibronectin type II modules of matrix metalloproteinase 2 (MMP-2).
references: Selective hydrolysis of triple-helical substrates by matrix metalloproteinase-2 and -9.
references: Distinct roles of catalytic and pexin-like domains in membrane-type matrix metalloproteinase (MMP)-mediated pro-MMP-2 activation and collagenolysis.
comment: This enzyme belongs to the peptidase family M10A. Although the catalytic residue and catalytic zinc are annotated, the detailed catalytic mechanism is still unclear.

Collagenase (Catalytic Domain)
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.390.10
catalytic domain: index.html

Seminal Fluid Protein PDC-109 (Domain B)
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.10.10.10

Hemopexin
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.110.10.10

Zinc
type: KeggCofactor
references: KEGG:C00038
compound type: heavy metal
references: CHEBI:29105
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Calcium
type: KeggCofactor
references: KEGG:C00076
compound type: divalent metal (Ca2+, Mg2+)
references: CHEBI:29108
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Gelatin type I
type: KeggSubstrate
references: KEGG:C00560
compound type: peptide/protein

Collagen type IV
type: KeggSubstrate
references: KEGG:C00335
compound type: peptide/protein

Collagen type V
type: KeggSubstrate
references: KEGG:C00421
compound type: peptide/protein

Collagen type VII
type: KeggSubstrate
references: KEGG:C02531
compound type: peptide/protein

Collagen type X
type: KeggSubstrate
references: KEGG:C02259
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

Protein
type: KeggProduct
references: KEGG:C00017
compound type: peptide/protein

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

1ck7A01
type: Pdb
references: 1ck7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ck7
cofactor binding residue: CYS 102;HIS 403;HIS 407;HIS 413(catalytic Zinc)
comment: mutant E404A

1qibA
type: Pdb
references: 1qib
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qib
catalytic residue: GLU 202
cofactor binding residue: ;HIS 201;HIS 205;HIS 211(catalytic Zinc)

1gxdA01
type: Pdb
references: 1gxd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gxd
cofactor binding residue: CYS 73;HIS 374;HIS 378;HIS 384(catalytic Zinc)
comment: mutant E375A

1gxdB01
type: Pdb
references: 1gxd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gxd
cofactor binding residue: CYS 73;HIS 374;HIS 378;HIS 384(catalytic Zinc)
comment: mutant E375A

1eakA01
type: Pdb
references: 1eak
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eak
cofactor binding residue: CYS 102;HIS 403;HIS 407;HIS 413(catalytic Zinc)
comment: mutant E404Q

1eakB01
type: Pdb
references: 1eak
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eak
cofactor binding residue: CYS 102;HIS 403;HIS 407;HIS 413(catalytic Zinc)
comment: mutant E404Q

1eakC01
type: Pdb
references: 1eak
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eak
cofactor binding residue: CYS 102;HIS 403;HIS 407;HIS 413(catalytic Zinc)
comment: mutant E404Q

1eakD01
type: Pdb
references: 1eak
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eak
cofactor binding residue: CYS 102;HIS 403;HIS 407;HIS 413(catalytic Zinc)
comment: mutant E404Q

Crystal structure of the haemopexin-like C-terminal domain of gelatinase A.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7583664
journal: Nat Struct Biol
volume: 2
pages: 938-42
published year: 1995
authors:
  item: Libson AM
  item: Gittis AG
  item: Collier IE
  item: Marmer BL
  item: Goldberg GI
  item: Lattman EE

The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8549817
journal: FEBS Lett
volume: 378
pages: 126-30
published year: 1996
authors:
  item: Gohlke U
  item: Gomis-Ruth FX
  item: Crabbe T
  item: Murphy G
  item: Docherty AJ
  item: Bode W

X-ray structure of gelatinase a catalytic domain complexed with a hydroxamate inhibitor.
type: BibliographicResource
journal: Croatica Chemica Acta
volume: 72
pages: 575-591
published year: 1999
authors:
  item: Dhanaraj V
  item: Williams_MG
  item: Ye_QZ
  item: Molina_F
  item: Johnson_LL
  item: Ortwine_DF
  item: Pavlovsky_A
  item: Rubin_JR
  item: Skeean_RW
  item: White_AD
  item: Humblet_C
  item: Hupe_DJ
  item: Blundell_TL
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10356396
journal: Science
volume: 284
pages: 1667-70
published year: 1999
authors:
  item: Morgunova E
  item: Tuuttila A
  item: Bergmann U
  item: Isupov M
  item: Lindqvist Y
  item: Schneider G
  item: Tryggvason K
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The second type II module from human matrix metalloproteinase 2: structure, function and dynamics.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10545322
journal: Structure Fold Des
volume: 7
pages: 1235-45
published year: 1999
authors:
  item: Briknarova K
  item: Grishaev A
  item: Banyai L
  item: Tordai H
  item: Patthy L
  item: Llinas M
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Gelatin-binding region of human matrix metalloproteinase-2: solution structure, dynamics, and function of the COL-23 two-domain construct.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11320090
journal: J Biol Chem
volume: 276
pages: 27613-21
published year: 2001
authors:
  item: Briknarova K
  item: Gehrmann M
  item: Banyai L
  item: Tordai H
  item: Patthy L
  item: Llinas M
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Tyrosine 36 plays a critical role in the interaction of the AB loop of tissue inhibitor of metalloproteinases-2 with matrix metalloproteinase-14.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11390386
journal: J Biol Chem
volume: 276
pages: 32966-70
published year: 2001
authors:
  item: Williamson RA
  item: Hutton M
  item: Vogt G
  item: Rapti M
  item: Knauper V
  item: Carr MD
  item: Murphy G

Specific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domain.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11513874
journal: FEBS Lett
volume: 503
pages: 158-62
published year: 2001
authors:
  item: Patterson ML
  item: Atkinson SJ
  item: Knauper V
  item: Murphy G

Substrate recognition by gelatinase A: the C-terminal domain facilitates surface diffusion.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11566806
journal: Biophys J
volume: 81
pages: 2370-7
published year: 2001
authors:
  item: Collier IE
  item: Saffarian S
  item: Marmer BL
  item: Elson EL
  item: Goldberg G

Endostatin binds to the catalytic domain of matrix metalloproteinase-2.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12023034
journal: FEBS Lett
volume: 519
pages: 147-52
published year: 2002
authors:
  item: Lee SJ
  item: Jang JW
  item: Kim YM
  item: Lee HI
  item: Jeon JY
  item: Kwon YG
  item: Lee ST

Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12032297
journal: Proc Natl Acad Sci U S A
volume: 99
pages: 7414-9
published year: 2002
authors:
  item: Morgunova E
  item: Tuuttila A
  item: Bergmann U
  item: Tryggvason K
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Solution structure and backbone dynamics of the catalytic domain of matrix metalloproteinase-2 complexed with a hydroxamic acid inhibitor.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12147339
journal: Biochim Biophys Acta
volume: 1598
pages: 10-23
published year: 2002
authors:
  item: Feng Y
  item: Likos JJ
  item: Zhu L
  item: Woodward H
  item: Munie G
  item: McDonald JJ
  item: Stevens AM
  item: Howard CP
  item: De Crescenzo GA
  item: Welsch D
  item: Shieh HS
  item: Stallings WC

Peptide ligands for the fibronectin type II modules of matrix metalloproteinase 2 (MMP-2).
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12486137
journal: J Biol Chem
volume: 278
pages: 12241-6
published year: 2003
authors:
  item: Trexler M
  item: Briknarova K
  item: Gehrmann M
  item: Llinas M
  item: Patthy L

Selective hydrolysis of triple-helical substrates by matrix metalloproteinase-2 and -9.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12642591
journal: J Biol Chem
volume: 278
pages: 18140-5
published year: 2003
authors:
  item: Lauer-Fields JL
  item: Sritharan T
  item: Stack MS
  item: Nagase H
  item: Fields GB

Distinct roles of catalytic and pexin-like domains in membrane-type matrix metalloproteinase (MMP)-mediated pro-MMP-2 activation and collagenolysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12878590
journal: J Biol Chem
volume: 278
pages: 38765-71
published year: 2003
authors:
  item: Jiang A
  item: Pei D

matrix metalloproteinase 2
type: KeggEnzyme

Analogue
compound: Peptide
pdb: 1eakA02
ligand het code: GLY-PRO-ALA-GLY-PRO-PRO-GLY-ALA

Analogue
compound: Peptide
pdb: 1eakD02
ligand het code: GLY-PRO-ALA-GLY-PRO-PRO-GLY-ALA

ReferenceForCatalyticMechanism
reference index: 4
reference section: p.1667-1669