3.4.24.7: interstitial collagenase
This is an abbreviated version!
For detailed information about interstitial collagenase, go to the full flat file.
Word Map on EC 3.4.24.7
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3.4.24.7
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metalloproteinases
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mmp-2
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metastasis
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gelatinase
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timp-1
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zymography
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endothelial
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gelatin
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angiogenesis
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cartilage
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fibrosis
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basement
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type-1
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stromelysins
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invasiveness
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arthritis
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dermal
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plasminogen
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gelatinolytic
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prommp-2
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proteinases
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integrins
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matrigel
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synovial
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pericellular
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fibrosarcoma
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mt-mmp
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fibrillar
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procollagen
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chondrocytes
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matrix-degrading
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collagenase-3
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progelatinase
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proenzyme
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invadopodia
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laminin-5
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analysis
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membrane-tethered
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pharmacology
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drug development
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triple-helical
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diagnostics
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photoaging
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medicine
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batimastat
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procollagenase
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podosomes
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furin
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hemopexin
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collagen-rich
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reck
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cortactin
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pro-matrix
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synthesis
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matrilysin
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emmprin
- 3.4.24.7
- metalloproteinases
- mmp-2
- metastasis
- gelatinase
- timp-1
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zymography
- endothelial
- gelatin
- angiogenesis
- cartilage
- fibrosis
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basement
- type-1
- stromelysins
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invasiveness
- arthritis
- dermal
- plasminogen
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gelatinolytic
- prommp-2
- proteinases
- integrins
- matrigel
- synovial
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pericellular
- fibrosarcoma
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mt-mmp
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fibrillar
- procollagen
- chondrocytes
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matrix-degrading
- collagenase-3
- progelatinase
- proenzyme
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invadopodia
- laminin-5
- analysis
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membrane-tethered
- pharmacology
- drug development
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triple-helical
- diagnostics
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photoaging
- medicine
- batimastat
- procollagenase
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podosomes
- furin
- hemopexin
-
collagen-rich
- reck
- cortactin
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pro-matrix
- synthesis
- matrilysin
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emmprin
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
3.4.24.7 interstitial collagenaseAdvanced search results
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results (Engineering
Engineering on EC 3.4.24.7 - interstitial collagenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DELTA243-340
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about 10% increase in turnover number and 9% increase in Km-value compared to wild-type enzyme with fTHP-3 as substrate
DELTA243-450
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the KM-value for the alpa1(I)772-786 triple-helical peptide is 3.3fold higher than that of the wild-type enzyme, the turnover number for this substrate is 2.5fold higher
E200A
catalytically inactive, but correctly folded mutant enzyme. MMP-1(Glu200Ala) has an intact HPX domain. The mutant can orient and help unwind the collagen triple helix, while the catalytic MMP-1 domain (MMP-1 CAT) cleaves the triple helix
L338A/H339A
site-directed mutagenesis, the mutant shows an increased collagenase activity, the MMP-1 L338A/H339A mutant corresponds to the appearance of a unique anticorrelated motion and decreased correlated motions
R183Q/W184W/T185T/N186K/N187D/F188T/R189T/E190G/Y191T
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mutation reduces collagenolytic activity about 10fold
V94G
constitutively active MMP-1 mutant. Expression of MMP-1 V94G in young skin in organ culture causes fragmentation and ultrastructural alterations of collagen fibrils similar to those observed in aged human skin in vivo. Expression of MMP-1 V94G in dermal fibroblasts cultured in three-dimensional collagen lattices causes substantial collagen fragmentation, which is markedly reduced by MMP-1 siRNA-mediated knockdown or MMP inhibitor MMI270. Fibroblasts cultured in MMP-1 V94G-fragmented collagen lattices display many alterations observed in fibroblasts in aged human skin, including reduced cytoplasmic area, disassembled actin cytoskeleton, impaired TGF-beta pathway, and reduced collagen production
additional information
additional information
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although increased MMP-1 levels are usually associated with angiogenesis in enabled proliferative endothelial cells, the exogenous addition of activated MMP-1 on lithium-arrested endothelial cells increases the number of endothelial cells positive for the senescent-associated-beta-galactosidase marker. Conversely, downregulation of MMP-1 expression by small interfering RNAs blunts the lithium-dependent increase in senescent-associated-beta-galactosidase positive cells. Lithium-induced MMP-1 expression is mediated neither by GSK3beta inhibition nor beta-catenin stabilization, lithium-dependent cell cycle arrest and the cell senescent phenotype in aortic endothelial cells are not triggered by inhibition of the inositol phosphate cycle. Induction molecular mechanism, overview
additional information
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construction of a chimeric enzyme, the exon 5 chimera, consisting primarily of MMP-1, with the region coded for by exon 5 replaced with the equivalent region of MMP-3, a noncollagenolytic MMP. Unlike MMP-3, the exon 5 chimera is capable of cleaving type I collagen, but the activity is only 2.2% of the trypsin-activated MMP-1. The kinetics for exon 5 chimera cleavage of two synthetic substrates display an MMP-3 phenotype, however, cleavage of gelatin is slightly impaired as compared to the parent enzymes. The KI-values for the exon 5 chimera complexed with synthetic inhibitors and N-terminal TIMP-2 show a more MMP-3-like behaviour. The exon 5 mutant shows a 2.9fold in the ratio of turnover number to Km-value with (7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-(3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2
additional information
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introduction of various lengths of MMP-1 segments into MMP-3, i.e. stromelysin 1, starting from the C-terminal end. MMP-3/MMP-1 chimeras and variants are overexpressed in Escherichia coli, folded from inclusion bodies and isolated as zymogens. The nine residues 183RWTNNFREY191 located between the fifth beta-strand and the second alpha-helix in the catalytic domain of MMP-1 are critical for the expression of collagenolytic activity
additional information
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MMP-1 enzyme inhibition and downregulation by short hairpin RNA, shRNA, reducing collagenase activity and angiogenesis of melanoma cells, but has no effect on primary tumor growth, xenograft modeling
additional information
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acid sphingomyelinase-deficient human fibroblasts fail to phosphorylate extracellular signal-regulated kinase, ERK, or upregulate MMP-1 mRNA and protein expression upon stimulation with interleukin-1 beta, overview. Transfection of acid sphingomyelinase restores MMP-1 production, while inhibition of acid sphingomyelinase with imipramine completely abrogates MMP-1 induction
additional information
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development of a piezoelectric immunosensor for matrix metalloproteinase-1 detection based on multilayered ultra-thin films composed by precursor layers of cationic poly(dimethyldiallylammonium) chloride and anionic poly(styrenesulfonate) with bound monolayer of antibodies, Layer by Layer self assembly technique, evaluation, overview
additional information
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disruption of the proximal AP-1-binding site in the promoter of MMP-1 severely impair MMP-1 transcription in response to bortezomib
additional information
identification of a common functional polymorphism in the matrix metalloproteinase-1 gene promoter, 1G or 2G at nucleotide -1607, in individuals with epidermolysis bullosa pruriginosa compared with non-itchy dominant dystrophic epidermolysis bullosa, recessive dystrophic epidermolysis bullosa and healthy controls, overview. Genetic variants of a common functional polymorphism in the matrix metalloproteinase-1 gene promoter do not account for the itchy skin phenotype, overview
additional information
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overexpression of both ADAMTS1 and MMP-1 together increases osteolytic bone metastases, while overexpression of ADAMTS or MMP-1 alone has no effect
additional information
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transfection of oral tongue squamous cell carcinoma cells with microRNA candidates, including hsa-miR-222, reduces the expression of MMP1 and SOD2 in the cells, direct targeting of hsa-miR-222 to specific sequences located in the 3'-untranslated regions of both MMP1 and SOD2, overview
additional information
incorporation of peptoid residues into collagen model triple-helical peptides and examination of MMP activities toward the peptomeric chimeras
additional information
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generation of specific recombinant human monoclonal antibody SP3, which is specific to the murine MMP-1 catalytic domain
additional information
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generation of specific recombinant human monoclonal antibody SP3, which is specific to the murine MMP-1 catalytic domain
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additional information
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transfection of rat myocard with a plasmid encoding MMP-1, DNA release and MMP1 expression, effects on myocard remodeling, overview. MMP-1 expression increases myocyte shortening and reduces Na+-Ca2+ exchange current, it decreases myocardial fibrosis and improves cardiac remodeling and function
