3.4.24.7: interstitial collagenase

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For detailed information about interstitial collagenase, go to the full flat file.

Reaction

Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at Gly775-/-Ile in the alpha1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue =

Synonyms

azocollase, collagen peptidase, collagen protease, collagenase, collagenase 1, collagenase A, collagenase MMP-1, collagenase-1, collagenolytic matrix metalloproteinase, EC 3.4.99.5, ect-MMP-14, Fibroblast collagenase, HSFC, kollaza, macrophage matrix metalloproteinase, matrix metalloproteinase 1, matrix metalloproteinase-1, matrix metalloproteinase-18, matrix-metalloproteinase-1, membrane-type 1-MMP, metallocollagenase, metalloproteinase-1, MMP-1, MMP-12, MMP-14, MMP-1A, mmp1, MT1-MMP, Myocardial collagenase, nucleolysin, soycollagestin, TC1, tumor collagenase, vertebrate collagenase

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.24 Metalloendopeptidases

                3.4.24.7 interstitial collagenase

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Results	in table
15	Activating Compound
38	AA Sequence
20	Application
1	CAS Registry Number
20	Cloned(Commentary)
2	Crystallization (Commentary)
7719	Disease/ Diagnostics
37	Expression
48	General Information
5	IC50 Value
181	Inhibitors
17	kcat/KM [mM/s]
111	Ki Value [mM]
52	KM Value [mM]
24	Localization
25	Metals/Ions
6	Molecular Weight [Da]
41	Natural Substrates/ Products (Substrates)
139	Organism
26	PDB ID
22	pH Optimum
7	pH Range
1	pH Stability
7	Posttranslational Modification
22	Protein Variants
11	Purification (Commentary)
1	Reaction
1	Reaction Type
137	Reference
2	Renatured (Commentary)
193	Source Tissue
6	Specific Activity [micromol/min/mg]
190	Substrates and Products (Substrate)
8	Subunits
161	Synonyms
9	Temperature Optimum [°C]
2	Temperature Stability [°C]
47	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.4.24.7 - interstitial collagenase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

hanging drop vapour-diffusion method. Crystal structure of the active form of human MMP-1 at 2.67 A resolution. This is a MMP-1 structure that is free of inhibitor and a water molecule essential for peptide hydrolysis is observed coordinated with the active site zinc

Homo sapiens

-

669889

small angle X-ray scattering

Homo sapiens

P03956

698886