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Information on EC 3.4.24.7 - interstitial collagenase
for references in articles please use BRENDA:EC3.4.24.7
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.24 Metalloendopeptidases
3.4.24.7 interstitial collagenase
IUBMB Comments
The enzyme takes its name from substrates of the interstitial collagen group - types I, II and III, all of which are cleaved in the helical domain. However, α-macroglobulins are cleaved much more rapidly. The enzyme is widely distributed in vertebrate animals. Type example of peptidase family M10
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 3.4.24.7
- metalloproteinases
- mmp-2
- metastasis
- gelatinase
- timp-1
-
zymography
- endothelial
- gelatin
- angiogenesis
- cartilage
- fibrosis
-
basement
- type-1
- stromelysins
-
invasiveness
- arthritis
- dermal
- plasminogen
-
gelatinolytic
- prommp-2
- proteinases
- integrins
- matrigel
- synovial
-
pericellular
- fibrosarcoma
-
mt-mmp
-
fibrillar
- procollagen
- chondrocytes
-
matrix-degrading
- collagenase-3
- progelatinase
- proenzyme
-
invadopodia
- laminin-5
- analysis
-
membrane-tethered
- pharmacology
- drug development
-
triple-helical
- diagnostics
-
photoaging
- medicine
- batimastat
- procollagenase
-
podosomes
- furin
- hemopexin
-
collagen-rich
- reck
- cortactin
-
pro-matrix
- synthesis
- matrilysin
-
emmprin
Reaction Schemes
showCleavage 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
mt1-mmp, mmp-14, interstitial collagenase, matrix metalloproteinase 1, collagenase-1, fibroblast collagenase, collagenase 1, vertebrate collagenase, membrane-type 1-mmp, matrix-metalloproteinase-1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
azocollase
-
-
-
-
collagen peptidase
-
-
-
-
collagen protease
collagenase
collagenase A
-
-
-
-
collagenase MMP-1
-
-
-
-
collagenase-1
EC 3.4.99.5
-
-
related
-
Fibroblast collagenase
-
-
-
-
kollaza
-
-
-
-
matrix metalloproteinase 1
matrix metalloproteinase-1
matrix metalloproteinase-18
-
-
-
-
metallocollagenase
-
-
-
-
metalloproteinase-1
-
-
-
-
MMP-1
MMP-1A
mmp1
MT1-MMP
Myocardial collagenase
-
-
-
-
nucleolysin
-
-
-
-
soycollagestin
-
-
-
-
TC1
-
-
-
-
vertebrate collagenase
-
-
-
-
collagen protease
-
-
-
-
collagenase
-
-
-
-
matrix metalloproteinase 1
-
-
-
-
matrix metalloproteinase-1
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-
-
-
matrix metalloproteinase-1
-
-
MMP-1
-
-
-
-
MMP-1
-
-
654953, 655414, 656272, 656898, 667132, 667138, 667858, 668108, 668666, 669246, 669889, 670882, 683221, 683330, 683445, 683451, 683633, 683988, 707015, 707312, 707982, 708187, 708231, 708406, 708425, 708432, 708511, 708587, 708788, 709025, 709234, 709289, 709345, 709370, 709482, 709591, 709669, 709685, 709700, 709789, 709813, 710246, 710259, 717678, 717876
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
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CAS REGISTRY NUMBER
COMMENTARY
9001-12-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(7-methoxycoumarin-4-yl)-acetyl-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(dinitrophenyl)-NH2 + H2O
(7-methoxycoumarin-4-yl)-acetyl-Arg-Pro-Lys-Pro-Val-Glu + Nva-Trp-Arg-Lys(dinitrophenyl)-NH2
-
Substrates: -
Products: -
Products: -
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-(3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly + Leu-(3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2
-
Substrates: -
Products: -
Products: -
?
(7-methoxycoumarin-4-yl)acetyl-Pro-cyclohexylalanine-Gly-Nve-His-Ala-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-NH2 + H2O
?
-
Substrates: degradation of synthetic substrate is pH-independent
Products: -
Products: -
?
(GP4Hyp)4-GPQGIAGQRGVVGL4Hyp(GP4Hyp)4-NH2 + H2O
(GP4Hyp)4-GPQG + IAGQRGVVGL4Hyp(GP4Hyp)4-NH2
Substrates: alpha1(I)772-786 THP
Products: -
Products: -
?
(GP4Hyp)4GPQ-Sar-IAGQRGVVG-Nle-GL4Hyp(GP4Hyp)4-NH2 + H2O
(GP4Hyp)4GPQ-Sar + IAGQRGVVG-Nle-GL4Hyp(GP4Hyp)4-NH2
Substrates: -
Products: -
Products: -
?
(GP4Hyp)4GPQ-Sar-IAGQRGVVGL4Hyp(GP4Hyp)4-NH2 + H2O
(GP4Hyp)4GPQ-Sar + IAGQRGVVGL4Hyp(GP4Hyp)4-NH2
Substrates: -
Products: -
Products: -
?
(GP4Hyp)4GPQGIAGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2 + H2O
(GP4Hyp)4GPQG + IAGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2
Substrates: the substrate is hydrolyzed at the Gly775-Ile776 bond by the enzyme
Products: -
Products: -
?
2,4-dinitrophenyl-Pro-beta-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(N-methyl-2-aminobenzoyl)-NH2 + H2O
?
Substrates: -
Products: -
Products: -
?
2,4-dinitrophenyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-NH2 + H2O
?
Frog
-
Substrates: -
Products: -
Products: -
?
2,4-dinitrophenyl-Pro-Leu-Ala-Leu-Trp-Ala-Arg-OH + H2O
?
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Ala-Gly-Ile-Ala-Gly-Gln-Arg-ethyl ester + H2O
acetyl-Pro-Ala-Gly + Ile-Ala-Gly-Gln-Arg-ethyl ester
Frog
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Gln-Gly-Ile-Ala-Gly-ethyl ester + H2O
acetyl-Pro-Gln-Gly + Ile-Ala-Gly-ethyl ester
Frog
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Arg-ethyl ester + H2O
acetyl-Pro-Gln-Gly + Ile-Ala-Gly-Gln-Arg-ethyl ester + H2O
Frog
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Arg-ethyl ester + H2O
acetyl-Pro-Gly-Pro-Gln-Gly + Ile-Ala-Gly-Gln-Arg-ethyl ester
Frog
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
acetyl-Pro-Leu-Gly-S-Leu-Leu-Gly ethyl ester + H2O
?
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-SCH[CH2CH(CH3)2CO]-Leu-Leu-OC2H5 + H2O
?
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-SCH[CH2CH(CH3)2]CO-Leu-Leu-OC2H5 + H2O
acetyl-Pro-Leu-Gly + HSCH[CH2CH(CH3)2]CO-Leu-Leu-OC2H5
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
butyloxycarbonyl-Pro-Ala-Gly-Ile-Ala-Gly-ethyl ester + H2O
butyloxycarbonyl-Pro-Ala-Gly + Ile-Ala-Gly-ethyl ester
Frog
-
Substrates: -
Products: -
Products: -
?
butyloxycarbonyl-Pro-Gln-Gly-Ile-Ala-Gly-ethyl ester + H2O
butyloxycarbonyl-Pro-Gln-Gly + Ile-Ala-Gly-ethyl ester
Frog
-
Substrates: -
Products: -
Products: -
?
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Ala-Gly-Gln-Gln
-
Substrates: -
Products: -
Products: -
?
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Gln-Arg-Gly-Val-Val-Gly-Leu-Hyp-NH2 + H2O
Gly-Pro-Gln-Gly + Ile-Ala-Gly-Gln-Gln-Arg-Gly-Val-Val-Gly-Leu-Hyp-NH2
-
Substrates: -
Products: -
Products: -
?
Human alpha2-macroglobulin + H2O
?
-
Substrates: cleavage site: Gly679-Leu680
Products: -
Products: -
?
human pregnancy zone protein + H2O
?
-
Substrates: cleavage sites: Gly685-Leu686, Gly687-Val688, Gly757-Ile758, Ala684-Leu684, and Ala685-Met686
Products: -
Products: -
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
Mca-Pro-Leu-Gly + Leu-Dpa-Ala-Arg-NH2
Substrates: -
Products: -
Products: -
?
Pro-Gln-Gly-Ile-Ala-Gly-Gln-Arg-ethyl ester + H2O
Pro-Gln-Gly + Ile-Ala-Gly-Gln-Arg-ethyl ester
Frog
-
Substrates: -
Products: -
Products: -
?
rat alpha1 macroglobulin + H2O
?
-
Substrates: cleavage site: His681-Leu682, Phe691-Leu692
Products: -
Products: -
?
rat alpha1-inhibitor 3 (27J) + H2O
?
-
Substrates: cleavage sites: Ala666-Val667
Products: -
Products: -
?
rat alpha1-inhibitor 3 (2J) + H2O
?
-
Substrates: cleavage sites: Pro683-Val684
Products: -
Products: -
?
rhodamine 6G-labeled KDP-6-aminohexanoic acid-GPLGIAGIG-6-aminohexanoic acid-PKGY + H2O
rhodamine 6G-labeled KDP-6-aminohexanoic acid-GPLG + IAGIG-6-aminohexanoic acid-PKGY
-
Substrates: fluorescent biosensor, substrate for matrix metalloproteinases MMP-2, MMP-9, MMP-14
Products: -
Products: -
?
[alpha1(I)]2alpha2(I)772-784 triple-helical peptide + H2O
?
-
Substrates: -
Products: -
Products: -
?
[alpha1(II)769-783] fluorogenic triple-helical peptide-3 + H2O
?
-
Substrates: -
Products: -
Products: -
?
[alpha1(II)769-783] fluorogenic triple-helical peptide-4 + H2O
?
-
Substrates: -
Products: -
Products: -
?
[alpha1(II)769-783] single-stranded peptide-3 + H2O
?
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
Frog
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
-
Substrates: very low activity
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
Frog
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
Frog
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
Frog
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
-
Substrates: very low activity
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
Frog
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
-
Substrates: very low activity
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
-
Substrates: -
Products: -
Products: -
?
Collagen + H2O
?
Frog
-
Substrates: native reconstituted guinea pig skin collagen fibrils
Products: -
Products: -
?
Collagen + H2O
?
-
Substrates: -
Products: two collagen fragments representing 77% and 23% respectively of the length of the collagen molecule
Products: two collagen fragments representing 77% and 23% respectively of the length of the collagen molecule
?
Collagen + H2O
?
-
Substrates: native reconstituted guinea pig skin collagen fibrils
Products: -
Products: -
?
Collagen + H2O
?
-
Substrates: cleavage sites: of calf skin alpha1(I) chain collagen Gly775-Ile776, of calf skin collagen alpha2(I) chain Gly775-Leu776, of human liver collagen alpha1(III)chain Gly775-Ile776
Products: -
Products: -
?
Collagen + H2O
?
-
Substrates: type X collagen, two cleavage sites, three products with 32000 Da, 18000 Da and 9000 Da chains
Products: -
Products: -
?
Collagen + H2O
?
-
Substrates: 183RWTNNFREY191, together with the C-terminal hemopexin domain, is essential for collagenolytic activity but additional structural elements in the catalytic domain are also required. These elements probably act in a concerted manner to cleave the collagen triple helix
Products: -
Products: -
?
Collagen + H2O
?
Substrates: natural collagen fascicles (termed extracellular matrix/ECM) from tendons of 6-months-old rats, degradation patterns of natural collagen-rich extracellular matrix by MMP-1 compared to MMP-13
Products: -
Products: -
?
Collagen + H2O
?
-
Substrates: below 30°C the enzyme catalyzes a small number of cleavages in the native collagen molecule with no loss in tertiary structure. Fragments of 75, 67, and 62% of the molecular length from the A end are formed. At 37°C and neutral pH, the enzyme degrades native collagen fibrils or molecules to peptides most of which are dialyzable
Products: -
Products: -
?
Collagen + H2O
?
Substrates: natural collagen fascicles (termed extracellular matrix/ECM) from tendons of 6-months-old rats, degradation patterns of natural collagen-rich extracellular matrix by MMP-1 compared to MMP-13. Cleavage sites identified in Col I-rich ECM under proteolytic degradation by MMP-1, overview
Products: -
Products: -
?
collagen I + H2O
?
-
Substrates: degradation
Products: -
Products: -
?
collagen I alpha-1 chain + H2O
?
-
Substrates: the overall enzymatic activity is higher on the alpha-2 chain for MMP-1 and MMP-2
Products: -
Products: -
?
collagen I alpha-1 chain + H2O
?
-
Substrates: MMP-14 ectodomain preferentially cleaves the alpha-1 chain
Products: -
Products: -
?
collagen I alpha-2 chain + H2O
?
-
Substrates: the overall enzymatic activity is higher on the alpha-2 chain for MMP-1 and MMP-2
Products: -
Products: -
?
collagen I alpha-2 chain + H2O
?
-
Substrates: MMP-14 ectodomain preferentially cleaves the alpha-1 chain
Products: -
Products: -
?
Collagen type III + H2O
?
Substrates: ability of MMP-1 to unwind triple-helical collagen
Products: -
Products: -
?
Collagen type III + H2O
?
Substrates: ability of MMP-1 to unwind triple-helical collagen. After binding the triple helix, the CAT domain can reorient to properly face the cleavage site. The dual Arg electrostatic ruler motif is modeled to be exposed in the type III collagen fibril. The two Arg residues found in type III collagen are conserved in the P5' and P17' subsites of types I and II collagen
Products: -
Products: -
?
collagen type IV alpha2 + H2O
?
Substrates: cleavage at sites L715 and T917
Products: -
Products: -
?
collagen type IV alpha2 + H2O
?
Substrates: cleavage at sites L715 and T917
Products: -
Products: -
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
-
Substrates: fluorogenic substrate
Products: -
Products: -
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
-
Substrates: fluorogenic substrate
Products: -
Products: -
?
Type I collagen + H2O
?
-
Substrates: production of type I collagen by periodontal ligament cells
Products: -
Products: -
?
Type I collagen + H2O
?
-
Substrates: -
Products: -
Products: -
?
Type I collagen + H2O
?
-
Substrates: a plasmin/MMP-10/MMP-1 proteolytic axis effectively enhances collagen type 1 degradation
Products: -
Products: -
?
type III collagen + H2O
?
-
Substrates: mechanism of interaction and cleavage of human type III collagen by fibroblast MMP-1 using a panel of recombinant human type III collagens containing engineered sequences in the vicinity of the cleavage site around residue I785, e.g. mutant FG-5015 I785P. Structural features of cleavage site determination in collagen type III, overview
Products: -
Products: -
?
fTHP-3 + H2O
additional information
-
-
Substrates: the fluorogenic triple-helical substrate mimics the behavior of the native collagen substrate and may be useful for the investigation of collagenase triple-helical activity
Products: the Gly-Leu bond is cleaved, the triple helix denatures and the two products generated are the single-stranded N-terminal peptide C6-(Gly-Pro-Hyp)5-Gly-Pro-Lys[(7-methoxycoumarin-4-yl)acetyl]-Gly-Pro-Gln-Gly and the single-stranded C-terminal peptide Leu-Arg-Gly-Gln-Lys-(2,4-dinitrophenyl)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
Products: the Gly-Leu bond is cleaved, the triple helix denatures and the two products generated are the single-stranded N-terminal peptide C6-(Gly-Pro-Hyp)5-Gly-Pro-Lys[(7-methoxycoumarin-4-yl)acetyl]-Gly-Pro-Gln-Gly and the single-stranded C-terminal peptide Leu-Arg-Gly-Gln-Lys-(2,4-dinitrophenyl)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
?
additional information
?
-
-
Substrates: relative rates of hydrolysis in decreasing order: GPQGIAGQ, PSYFLNAG, GNVGLAGA
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme prefers very lipophilic sequences
Products: -
Products: -
?
additional information
?
-
-
Substrates: matrix metalloproteinase 1 interacts with neuronal integrins and stimulates dephosphorylation of Akt and neuronal death through a non-proteolytic mechanism. MMP-1 might contribute to the neuronal damage which occurs in association with degenerative and inflammatpry conditions characterized by elevated levels of this proteinase
Products: -
Products: -
?
additional information
?
-
-
Substrates: ligation of keratinocyte alpha2beta1 integrin by type 1 collagen induces expression of matrix metalloproteinase-1. The MMP-1 activity is required for the alpha2beta1 integrin-dependent migration of primary keratinocytes across collagenous matrices. MMP-1 binds to the I domain of the alpha2 intergrin subunit
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-1 is involved in intestinal re-epithelization in vivo and is upregulated by cytokines relevant in wound repair
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-1 is a single effector of the Raf/MEK/ERK signaling cascade, that prevents progression of melanoma from a primary to metastatic tumor
Products: -
Products: -
?
additional information
?
-
-
Substrates: substance P up-regulates matrix metalloproteinase-1 and down-regulates collagen in human lung fibroblast, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP1 expression is increased in Xeroderma pigmentosum, a rare, recessively inherited genetic disease characterized by skin cancer proneness and premature aging in photoexposed area
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme regulation on expression and protein levels, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-1 cleaves a specific glycine-isoleucine or glycine-leucine bond in fibrillar collagens, despite the presence of this sequence in other parts of the protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: active MMP-10, EC 3.4.24.22, does not cleave collagen type 1 directly, it does activate the collagenase MMP-1
Products: -
Products: -
?
additional information
?
-
-
Substrates: matrix metalloproteinases are endopeptidases capable of cleaving various components of extracellular matrix
Products: -
Products: -
?
additional information
?
-
Substrates: MMP-1 preferentially binds the alpha2(I) chain
Products: -
Products: -
?
additional information
?
-
Substrates: several different peptoid residues are incorporated into triple helical substrates at subsites P3, P1, P1', and P10' individually or in combination, and the effects of the peptoid residues are evaluated on the activities of full-length MMP-1 and other MMPs, collagenolytic matrix metalloproteinase activities toward peptomeric triple-helical substrates, overview. Most peptomers show little discrimination between MMPs. A peptomer containing N-methyl Gly (sarcosine) in the P1' subsite and N-isobutyl Gly (Nle) in the P10' subsite is not hydrolysed by MMP-1. Also no activity with (GP4Hyp)4-GPQG-Sar-AGQRGVVGL4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4GPQG-Sar-AGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4G-Sar-QGIAGQRGVVGL4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4GPQGWAGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4-GPQG-NIle-AGQRGVVGL4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4GPQG-Sar-AGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4GP-Lys(Mca)-G-Sar-AGQRGV-Lys(Dnp)-GNle-4Hyp(GP4Hyp)4-NH2 and Ac-(GP4Hyp)4-GP-Lys(Mca)-G-Sar-AGQRGV-Lys(Dnp)G-Nle-4Hyp(GP4Hyp)4-NH2, 4Hyp is hydroxyproline. The P10' subsite is important for collagenous substrate interaction with MMP-1, and this interaction occurs via the HPX domain. Molecular dynamics (MD) simulations, model of MMP-1 with the alpha1(I)772-786 THP, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: myocardial matrix degradation by MMP-1 induced by thyroid hormone through enzyme activation, enzyme regulation involving suppression of tissue inhibitors of matrix metalloproteinases TIMPs and distribution, overview
Products: -
Products: -
?
additional information
?
-
Substrates: proteomic analysis of MMP-1 activity using LC-MS/MS analysis
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
collagen I + H2O
?
-
Substrates: degradation
Products: -
Products: -
?
Collagen type III + H2O
?
Substrates: ability of MMP-1 to unwind triple-helical collagen
Products: -
Products: -
?
Type I collagen + H2O
?
-
Substrates: production of type I collagen by periodontal ligament cells
Products: -
Products: -
?
Type I collagen + H2O
?
-
Substrates: -
Products: -
Products: -
?
Type I collagen + H2O
?
-
Substrates: a plasmin/MMP-10/MMP-1 proteolytic axis effectively enhances collagen type 1 degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: matrix metalloproteinase 1 interacts with neuronal integrins and stimulates dephosphorylation of Akt and neuronal death through a non-proteolytic mechanism. MMP-1 might contribute to the neuronal damage which occurs in association with degenerative and inflammatpry conditions characterized by elevated levels of this proteinase
Products: -
Products: -
?
additional information
?
-
-
Substrates: ligation of keratinocyte alpha2beta1 integrin by type 1 collagen induces expression of matrix metalloproteinase-1. The MMP-1 activity is required for the alpha2beta1 integrin-dependent migration of primary keratinocytes across collagenous matrices. MMP-1 binds to the I domain of the alpha2 intergrin subunit
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-1 is involved in intestinal re-epithelization in vivo and is upregulated by cytokines relevant in wound repair
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-1 is a single effector of the Raf/MEK/ERK signaling cascade, that prevents progression of melanoma from a primary to metastatic tumor
Products: -
Products: -
?
additional information
?
-
-
Substrates: substance P up-regulates matrix metalloproteinase-1 and down-regulates collagen in human lung fibroblast, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP1 expression is increased in Xeroderma pigmentosum, a rare, recessively inherited genetic disease characterized by skin cancer proneness and premature aging in photoexposed area
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme regulation on expression and protein levels, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-1 cleaves a specific glycine-isoleucine or glycine-leucine bond in fibrillar collagens, despite the presence of this sequence in other parts of the protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: active MMP-10, EC 3.4.24.22, does not cleave collagen type 1 directly, it does activate the collagenase MMP-1
Products: -
Products: -
?
additional information
?
-
-
Substrates: matrix metalloproteinases are endopeptidases capable of cleaving various components of extracellular matrix
Products: -
Products: -
?
additional information
?
-
-
Substrates: myocardial matrix degradation by MMP-1 induced by thyroid hormone through enzyme activation, enzyme regulation involving suppression of tissue inhibitors of matrix metalloproteinases TIMPs and distribution, overview
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cobalt
substitution of zinc by Co(II) maintains the hydrogen bonding interactions in the catalytic site. The first coordination-sphere histidine residues for both the catalytic and structural Zn(II) sites of MMP-1 have a similar orientation. The replacement does not show a substantial effect on angles between the metal center and its coordinated residues
Zinc
Zn2+
Ca2+
-
both collagen and globular protein substrates of collagenase may bind Ca2+ and Zn2+ in the active site
Zinc
the orientation of residue Glu200 is stabilized by interactions with the catalytic Zn(II) first-coordinating sphere residue His203, and a second sphere, Val196 residue
Zinc
protonation of the scissile bond nitrogen occurs via proton transfer from a Zn(II)-coordinated hydroxide rather than from a solvent water molecule. Following C-N bond cleavage, the C-terminus remains coordinated to the catalytic Zn(II), while the N-terminus forms a hydrogen bond with a solvent water molecule
Zn2+
-
both collagen and globular protein substrates of collagenase may bind Ca2+ and Zn2+ in the active site
Zn2+
in presence of 5 mM Ca2+, optimum concentration 0.001 mM, decrease in activity above
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-phenyl)-carbamic acid tert-butyl ester
-
-
2-[benzyl([[(2-methylphenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
-
2-[benzyl([[(4-chlorophenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
-
2-[benzyl([[(4-fluorophenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
-
2-[benzyl([[(4-methylphenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
-
3-[((1R,4S)-7,7-Dimethyl-2-oxo-bicyclo[2.2.1]hept-1-ylmethanesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(2,4-Dinitro-phenylsulfanyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(2,5-Dichloro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(3-Chloro-4-ethylamino-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(3-Chloro-4-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(4-Chloro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(4-Fluoro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(5-Dimethylamino-naphthalene-1-sulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(Heptadecachlorooctane-1-sulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[3-(2,4-Dichloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-(3,4-Dichloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-(4-Chloro-phenylsulfonyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-(4-Fluoro-phenylsulfonyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[[3-[3-(4-chloro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[[3-[3-(4-fluoro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[[4-[3-(4-chloro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[[4-[3-(4-fluoro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
-
pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
astragaloside IV
AST, inhibits matrix metalloproteinase-1 in photoaging skin. Astragaloside IV is one of the major active compoxadnents extracted from Astragalus membranaceus. Effects of AST against collagen reducxadtion in UV-induced skin aging in human skin fibroblasts, and mechanism of multiple anti-photoaging effects, overview
benzo[a]pyrene
increases the mRNA levels of matrix metalloproteinases MMP-1, MMP-2, MMP-3, and MMP-9 in vascular smooth muscle cells and promotes the migration and invasion of cells
C3H7-POOH-Ile-Trp-NHMe
-
phosphonamidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
ClCH2CO-(N-OH)Leu-Ala-Gly-NH2
-
2-5 mM, 25°C, pH 7.4, Tris buffer, strong irreversible inhibition, inhibition increases with higher temperatures and inhibitor concentration
dexamethasone
-
significantly decreases active MMP-1 level and inhibits active MMP-1
disodium isostearyl 2-O-L-ascorbyl phosphate
-
i.e. disodium 2-(1,3,3-trimethyl-n-butyl)-5,7,7-trimethyl-n-octyl-L-ascorbyl phosphate or VCP-IS-2Na, an amphiphilic vitamin C derivative, increases proliferation of normal human skin fibroblasts, NHDFs and NB1RGBs, by 123% and 135% and inhibits MMP-1 production by a maximum of 19% and 11% in NHDF and NB1RGB cells at 0.05 mM, respectively
epigallocatechin gallate
competitive. the galloyl group is important for inhibitory activity
EtO-POOH-CH2-Leu-Trp-NHMe
-
pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
EtO-POOH-Ile-Ala-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
EtO-POOH-Ile-Ala-Gly-Gln-Arg-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
EtO-POOH-Ile-Ala-Gly-Glu-Arg(NO2)-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
EtO-POOH-Ile-Ala-Gly-Glu-Arg-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
EtO-POOH-Ile-Leu-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
EtO-POOH-Ile-Trp-NHMe
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
EtO-POOH-Ile-Tyr(OBzl)-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
EtO-POOH-Ile-Tyr-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
exopolysaccharide
-
obtained from mycelial culture of Grifola frondosa HB0071 may contribute to inhibitory action in photoaging skin by reducing the MMP-1-related matrix degradation system
-
hexyl-POOH-CH2-Leu-Trp-NHMe
-
pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
hexyl-POOH-Leu-Trp-NHMe
-
pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
hexyl-POOH-O-Leu-Trp-NHMe
-
pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
N-2-methylphenylsulfonylureido-N-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-2-methylphenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-2-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-2-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-2-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-4-chlorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-4-chlorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine
-
-
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
-
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-4-fluorophenylsulfonylureido-N-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-4-fluorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-4-fluorophenylsulfonylureido-N-[(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
-
N-4-fluorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-4-fluorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
-
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-4-methylphenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-4-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-4-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-Hydroxy-3-[(4-methoxy-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(2,4,6-trimethyl-benzenesulfonyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(3-trifluoromethyl-benzenesulfonyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(nonachlorobutane-1-sulfonyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-pentafluorobenzenesulfonyl-amino]-propionamide
-
-
N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-o-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-p-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-phenylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-o-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-p-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-phenylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
N-phenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-phenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-phenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
naphthoyl-Gly-PSI[POOHCH2]-Leu-Trp-NHBzl
-
pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
PAI-1
-
functions as an upstream regulator of a MMP-1-initiated collagenolytic phenotype, it blocks conversion of MMP-1 to its active form. Neutralization of endogenous PAI-1 with function blocking antibodies accelerates both collagenolysis and activation of MMP-1
-
pedunculagin
potent inhibitory effect on MMP-1 and the increased type-I procollagen synthesis in ultraviolet B-induced human fibroblast
phthaloyl-Gly(P)-Ile-Trp-(R)NHCH-(Me)Ph
-
phosphonamidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
phthaloyl-Gly(P)-Ile-Trp-NHBzl
-
50 µM, 25°C, pH 7.4, Tris buffer, reversible inhibition, protects the enzyme partially from inactivation by ClCH2CO-(N-OH)Leu-Ala-Gly-NH2
phthaloyl-Gly-PSI[POOHNH]-Ile-Trp-(S)NHCH-(Me)Ph
-
phosphonamidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
tissue inhibitor of matrix metalloproteinase-2
-
0.1 microM, inhibits both protease activity and migration in a 3-dimensional cross-linked collagen matrix
-
[3-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-phenyl]-carbamic acid tert-butyl ester
-
-
[4-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-phenyl]-carbamic acid tert-butyl ester
-
-
[5-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-2-methoxy-phenyl]-carbamic acid tert-butyl ester
-
-
TIMP-1
-
specific MMP-1 inhibitor. Inhibition of p38 signaling by SB203580 increases TIMP-1 secretion, as well as infection with Mycobacterium tuberculosis, overview
-
TIMP-1
-
no apparent regulation of the expression of TIMP-1 by either tumor necrosis factor or enamel matrix derivative
-
TIMP-1
-
TIMP-1 from brain is upregulated in in the infarcted tissue compared to healthy control areas, overview
-
TIMP-1
-
expression profile of MMPs/TIMP-1 after myocardial infarction, angiotensin II receptor blockade improves MMPs/TIMP-1 balance, overview
-
TIMP-2
-
expression of TIMP-2 in addition to bisphosphonate treatment markedly reduces the number of osteolytic lesions in breast cancer and increases overall survival compared with treatment with bisphosphonates alone
-
tissue inhibitor of matrix metalloproteinase-1
-
is not influenced by substance P
-
additional information
-
no inhibition of MMP-1 by BAY 12-9566, quantitative structure-activity relationship analysis of some 5-amino-2-mercapto-1,3,4-thiadiazole based inhibitors, overview
-
additional information
-
human tissue factor pathway inhibitor-2 does not bind or inhibit activated matrix metalloproteinase-1
-
additional information
-
the JNK inhibitor SP600125 inhibits rapamycin-induced MMP-1 gene transactivation and AP-1/DNA interactions, overview
-
additional information
-
panduratin A, isolated from Kaempferia pandurata, suppresses MMP-1 expression and enhances the expression of type-1 procollagen in UV-irradiated skin fibroblasts, overview
-
additional information
-
after hyperglycaemic treatment of keratinocytes, expression of matrix metalloproteinase-1 and alpha2beta1 integrin is significantly downregulated
-
additional information
-
not inhibitory: tissue inhibitor of matrix metalloproteinase-1
-
additional information
-
human fibroblast inhibitor effective against all vertebrate collagenases tested
-
additional information
platelet-derived growth factor (PDGF) treatment recruits BSMCs to injured sites and strengthens the effect of BMSCs on skin wound by suppressing activity of MMP-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15-deoxy-DELTA12,14-prostaglandin J2
-
treatment of with 30 mM of 15-deoxy-DELTA12,14-prostaglandin J2 increases the expression of heme oxygenase-1, which precedes the induction of matrix metalloproteinases. The 15-deoxy-DELTA12,14-prostaglandin J2-induced upregulation of MMP-1 is abrogated by the heme oxygenase-1 inhibitor zinc protoporphyrin IX as well as introduction of heme oxygenase-1 short interfering RNA
4-aminophenylmercuric acetate
-
MMP-1 from synovial fibroblasts is activated with 10 mM 4-aminophenylmercuric acetate in 0.1 N NaOH at 37 °C for 3 h
glucose
-
presence of high glucose levels and interferon gamma in culture medium have a synergistic effect on the expression of matrix metalloproteinases MMP-1, MMP-9 and interleukin-1beta. High glucose also enhances interferon gamma-induced priming effect on lipopolysaccharide-stimulated MMP-1 secretion. High glucose and interferon gamma exert the synergistic effect on MMP-1 expression by enhancing STAT1 phosphorylation and STAT1 transcriptional activity
interferon gamma
-
presence of high glucose levels and interferon gamma in culture medium have a synergistic effect on the expression of matrix metalloproteinases MMP-1, MMP-9 and interleukin-1beta. High glucose also enhances interferon gamma-induced priming effect on lipopolysaccharide-stimulated MMP-1 secretion. High glucose and interferon gamma exert the synergistic effect on MMP-1 expression by enhancing STAT1 phosphorylation and STAT1 transcriptional activity
-
thyroid hormone
-
thyroid hormone induces myocardial matrix degradation by MMP-1 activation
-
additional information
-
substance P up-regulates matrix metalloproteinase-1 and down-regulates collagen in human lung fibroblast, overview
-
additional information
-
proteasome blockade, regardless of the inhibitor used, e.g. proteasome inhibitor I, MG-132, lactacystin, or bortezomib, decreases the production of type I collagen and TIMP-1 and up-regulates that of MMP-1, overview
-
additional information
-
essential role of activator protein-1 activation in constitutive MMP1 overexpression in Xeroderma pigmentosum-C primary fibroblasts
-
additional information
-
rapamycin-induced MMP-1 gene transactivation and AP-1/DNA interactions, rapamycin significantly enhances the expression of interstitial collagenase at the protein and mRNA levels and transcriptionally, rapamycin efficiently activates activator protein-1, AP-1-driven transcription by rapidly inducing c-jun/AP-1 phosphorylation with activation of the c-Jun N-terminal kinase cascade, resulting in enhanced binding of AP-1-DNA complex formation and AP-1-dependent gene transactivation, overview
-
additional information
-
disruption of caveolae by addition of methyl-beta-cyclodextrin results in a dramatic decline in both motility and invasion abilities of cells with concomitant increase in secreted MMP-2 expression and expression levels of MMP-1 and MMP-9
-
additional information
-
active MMP-10 does not cleave collagen type 1 directly, it does activate the collagenase MMP-1, EC 3.4.24.7. The ability of active MMP-10 to superactivate MMP-1 creates a plasmin/MMP-10/MMP-1 proteolytic axis effectively enhances collagen type 1 degradation
-
additional information
-
dexamethasone induces myocardial matrix degradation by MMP-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.013
2,4-dinitrophenyl-Pro-beta-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(N-methyl-2-aminobenzoyl)-NH2
pH 7.5, 40°C
0.63
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Gln-Arg-Gly-Val-Val-Gly-Leu-Hyp-NH2
-
wild-type enzyme
0.0037
[alpha1(I)]2alpha2(I)772-784 triple-helical peptide
-
mutant enzyme E200A
-
0.0612
[alpha1(II)769-783] fluorogenic triple-helical peptide-3
-
wild-type enzyme
-
0.0208
[alpha1(II)769-783] fluorogenic triple-helical peptide-4
-
wild-type enzyme
-
0.00086
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 1-protonated
-
0.0011
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 1-protonated
-
0.0075
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 0-protonated
-
0.016
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 2-protonated
-
0.045
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 0-protonated
-
0.12
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 3-protonated
-
0.17
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 2-protonated
-
0.74
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 3-protonated
-
0.00025
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 1-protonated
-
0.0024
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 2-protonated
-
0.0028
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 1-protonated
-
0.004
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 2-protonated
-
0.01
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 0-protonated
-
0.14
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 3-protonated
-
0.46
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 3-protonated
-
0.53
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 0-protonated
-
additional information
additional information
-
kinetics with wild-type and mutant FG-5015 I785P type III collagen substrates, overview
-
additional information
additional information
kinetic analysis, Michaelis-Menten kinetic model
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.51
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Gln-Arg-Gly-Val-Val-Gly-Leu-Hyp-NH2
-
wild-type enzyme
0.08
[alpha1(II)769-783] fluorogenic triple-helical peptide-3
-
wild-type enzyme
-
0.04
[alpha1(II)769-783] fluorogenic triple-helical peptide-4
-
wild-type enzyme
-
0.21
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 0-protonated
-
0.3
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 1-protonated
-
0.43
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 2-protonated
-
0.65
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 3-protonated
-
0.66
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 1-protonated
-
1.83
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 2-protonated
-
4.56
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 0-protonated
-
10.41
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 3-protonated
-
0.014
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 2-protonated
-
0.089
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 1-protonated
-
0.54
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 3-protonated
-
0.79
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 2-protonated
-
4.09
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 3-protonated
-
5.44
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 1-protonated
-
16.9
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 0-protonated
-
58.61
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 0-protonated
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.88
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 3-protonated
-
2.5
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 2-protonated
-
28
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 0-protonated
-
88
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 3-protonated
-
100
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 0-protonated
-
120
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 2-protonated
-
360
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 1-protonated
-
630
collagen I alpha-1 chain
-
pH not specified in the publication, 37°C, MMP-1: 1-protonated
-
1.2
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 3-protonated
-
3.5
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 2-protonated
-
30
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 3-protonated
-
110
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 0-protonated
-
330
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 2-protonated
-
350
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 1-protonated
-
1600
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 0-protonated
-
1900
collagen I alpha-2 chain
-
pH not specified in the publication, 37°C, MMP-1: 1-protonated
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00002
(3-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-phenyl)-carbamic acid tert-butyl ester
-
-
0.000162
2-[benzyl([[(2-methylphenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
pH 6.0, 37°C
0.000143
2-[benzyl([[(4-chlorophenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
pH 6.0, 37°C
0.000135
2-[benzyl([[(4-fluorophenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
pH 6.0, 37°C
0.00017
2-[benzyl([[(4-methylphenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
pH 6.0, 37°C
0.000057
3-[((1R,4S)-7,7-Dimethyl-2-oxo-bicyclo[2.2.1]hept-1-ylmethanesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000027
3-[(2,4-Dinitro-phenylsulfanyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.00005
3-[(2,5-Dichloro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000031
3-[(2-Hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-benzoic acid
-
-
0.00005
3-[(3-Chloro-4-ethylamino-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.00003
3-[(3-Chloro-4-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000024
3-[(4-Bromo-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000023
3-[(4-Chloro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000021
3-[(4-Fluoro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000089
3-[(5-Dimethylamino-naphthalene-1-sulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000077
3-[(Heptadecachlorooctane-1-sulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000018
3-[3-(2,4-Dichloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000036
3-[3-(3,4-Dichloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000026
3-[3-(3-Chloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000024
3-[3-(4-Chloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.00004
3-[3-(4-Chloro-phenylsulfonyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000021
3-[3-(4-Fluoro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000047
3-[3-(4-Fluoro-phenylsulfonyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000057
3-[[3-[3-(4-chloro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000055
3-[[3-[3-(4-fluoro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000056
3-[[4-[3-(4-chloro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000055
3-[[4-[3-(4-fluoro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.00003
4-[(2-Hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-benzoic acid
-
-
0.002
C3H7-POOH-Ile-Trp-NHMe
-
phosphonamidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
0.004
EtO-POOH-CH2-Leu-Trp-NHMe
-
pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
0.12
EtO-POOH-Ile-Ala-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
0.5
EtO-POOH-Ile-Ala-Gly-Gln-Arg-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
0.27
EtO-POOH-Ile-Ala-Gly-Glu-Arg(NO2)-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
0.4
EtO-POOH-Ile-Ala-Gly-Glu-Arg-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
0.045
EtO-POOH-Ile-Leu-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
0.012
EtO-POOH-Ile-Trp-NHMe
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
0.002
EtO-POOH-Ile-Tyr(OBzl)-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
0.02
EtO-POOH-Ile-Tyr-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
0.3
hexyl-POOH-O-Leu-Trp-NHMe
-
pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
0.000039
N-2-methylphenylsulfonylureido-N-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37°C
0.000036
N-2-methylphenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37°C
0.000038
N-2-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37°C
0.000029
N-2-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37°C
0.000015
N-2-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37°C
0.000024
N-4-chlorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37°C
0.000024
N-4-chlorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37°C
0.00019
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine
-
pH 6.0, 37°C
0.00002
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37°C
0.00023
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
pH 6.0, 37°C
0.000014
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37°C
0.000025
N-4-fluorophenylsulfonylureido-N-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37°C
0.000021
N-4-fluorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37°C
0.0002
N-4-fluorophenylsulfonylureido-N-[(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
pH 6.0, 37°C
0.000021
N-4-fluorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37°C
0.000013
N-4-fluorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37°C
0.000017
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37°C
0.00018
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
pH 6.0, 37°C
0.000011
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37°C
0.000032
N-4-methylphenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37°C
0.00003
N-4-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37°C
0.000018
N-4-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37°C
0.000024
N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37°C
0.000015
N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37°C
0.000043
N-Hydroxy-3-[(2-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.00005
N-Hydroxy-3-[(3-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000032
N-Hydroxy-3-[(4-iodo-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000023
N-Hydroxy-3-[(4-methoxy-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.00005
N-Hydroxy-3-[(4-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000035
N-Hydroxy-3-[(4-nitro-benzyl)-(2,4,6-trimethyl-benzenesulfonyl)-amino]-propionamide
-
-
0.000028
N-Hydroxy-3-[(4-nitro-benzyl)-(2-nitro-phenylsulfanyl)-amino]-propionamide
-
-
0.000006
N-Hydroxy-3-[(4-nitro-benzyl)-(3-trifluoromethyl-benzenesulfonyl)-amino]-propionamide
-
-
0.000024
N-Hydroxy-3-[(4-nitro-benzyl)-(4-nitro-phenylsulfanyl)-amino]-propionamide
-
-
0.000069
N-Hydroxy-3-[(4-nitro-benzyl)-(nonachlorobutane-1-sulfonyl)-amino]-propionamide
-
-
0.000055
N-Hydroxy-3-[(4-nitro-benzyl)-(quinoline-8-sulfonyl)-amino]-propionamide
-
-
0.00003
N-Hydroxy-3-[(4-nitro-benzyl)-(toluene-4-sulfonyl)-amino]-propionamide
-
-
0.000002
N-Hydroxy-3-[(4-nitro-benzyl)-pentafluorobenzenesulfonyl-amino]-propionamide
-
-
0.000027
N-Hydroxy-3-[(4-nitro-benzyl)-phenylmethanesulfonyl-amino]-propionamide
-
-
0.000023
N-Hydroxy-3-[(4-nitro-benzyl)-trichloromethanesulfonyl-amino]-propionamide
-
-
0.000022
N-Hydroxy-3-[(4-nitro-benzyl)-trifluoromethanesulfonyl-amino]-propionamide
-
-
0.000055
N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-o-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
0.00005
N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-p-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
0.000062
N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-phenylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
0.00007
N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-o-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
0.000057
N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-p-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
0.000069
N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-phenylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
0.000082
N-Hydroxy-3-[(naphthalene-1-sulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000065
N-Hydroxy-3-[(naphthalene-2-sulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000069
N-Hydroxy-3-[1-(4-nitro-benzyl)-3-o-tolylsulfonyl-ureido]-propionamide
-
-
0.000042
N-Hydroxy-3-[1-(4-nitro-benzyl)-3-p-tolylsulfonyl-ureido]-propionamide
-
-
0.000052
N-Hydroxy-3-[1-(4-nitro-benzyl)-3-phenylsulfonyl-ureido]-propionamide
-
-
0.000038
N-Hydroxy-3-[dimethylsulfamoyl-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000025
N-phenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37°C
0.000015
N-phenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37°C
0.000013
N-phenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37°C
0.002
phthaloyl-Gly-PSI[POOHNH]-Ile-Trp-(S)NHCH-(Me)Ph
-
phosphonamidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
0.00005
[4-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-phenyl]-carbamic acid tert-butyl ester
-
-
0.000024
[5-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-2-methoxy-phenyl]-carbamic acid tert-butyl ester
-
-
additional information
additional information
-
Ki-values above 250 nM are determined for N-4-fluorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine, N-4-chlorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine, N-phenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine, N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine, N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine, N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine, N-4-fluorophenylsulfonylureido-N-(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine, N-4-chlorophenylsulfonylureido-N-(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine, N-4-methylphenylsulfonylureido-N-[(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine, N-4-fluorophenylsulfonylureido-N-[(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine
-
additional information
additional information
-
inhibition kinetics using diverse variants of 5-amino-2-mercapto-1,3,4-thiadiazoles, overview
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
activity in primary lung fibroblast cell lines in presence or absence of substance P, overview
additional information
-
quantitative MMP-1 expression analysis by RT-PCR in presence or absence of enzyme inhibitors
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
7.4
7.5
7.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8 - 9
-
pH 5.8: about 30% of maximal activity, pH 9.0: about 45% of maximal activity
6 - 9.2
6.5 - 9.5
-
pH 6.5: about 65% of maximal activity, pH 9.5: about 60% of maximal activity
6 - 9.2
-
degradation of collagen I: over the whole pH range investigated the proteolytic activity on the alpha2 chains is higher than for the alpha1 chain. Difference is large at alkaline pH (40fold at pH 9.2) and it decreases as the pH decreases toward the physiological value where the enzymatic processing of the alpha2 chain is only 4times higher than for the alpha1 chain. Difference remains essentially unchanged down to pH 6.3
6 - 9.2
-
degradation of collagen I: at pH 7.5 a 10fold higher activity is observed toward the alpha-2 chain, whereas a very similar value for the two chains is detected at pH 7.0. At pH lower 7.0 the overall enzymatic activity toward the alpha-1 chain increases, whereas the processing of the alpha-2 chain remains essentially constant between pH 7.3 and 6.0
6 - 9.2
-
degradation of synthetic substrate: overall enzymatic activity of ect-MMP-14 displays a pH dependence characterized by maximum efficiency at pH 7.0, which decreases upon both pH increase and pH decrease
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
95818, 95821, 95823, 95824, 95825, 95826, 95829, 95830, 95832, 95833, 95834, 95835, 95838, 654602, 654848, 654919, 654953, 655414, 655501, 655985, 656016, 656272, 656898, 665844, 667132, 667138, 667214, 667833, 667858, 668108, 668666, 668978, 669246, 669276, 669432, 669889, 670882, 683221, 683330, 683445, 683451, 683633, 683988, 695964, 696966, 697019, 697142
-
-
brenda
-
707015, 707312, 707313, 707397, 707648, 707958, 707982, 708187, 708231, 708406, 708425, 708432, 708511, 708587, 708788, 709025, 709234, 709289, 709345, 709370, 709415, 709482, 709591, 709669, 709685, 709700, 709789, 709813, 709913, 710246, 710259, 717074, 717678, 717876
-
-
brenda
-
733049, 733225, 733743, 734377, 752420, 752753, 754720, 754756, 755250, 769259, 770448, 771049, 773677, 774983, 775256
UniProt
brenda
DNA repair-deficient/cancer-prone xeroderma pigmentosum group C patients, Caucasian and Black
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
cell line JJ, increased MMP1 expression in chondrosarcoma, mechanism, overview
brenda
-
mucosa, immunohistochemic analysis of MMP-1 and TIMP-1 levels, overview. Overall plasma levels of MMP-1 and TIMP-1 in ulcerative colitis patients are significantly higher than those of the control group
brenda
-
acceleration of matrix metalloproteinase-1 production by oxidized low-sensity lipoprotein and 4-hydroxynonenal
brenda
-
MMP-1 is expressed by migrating enterocytes bordering intestinal ulcers. In the fetal gut model, MMP-1 expression by migrating enterocytes is detected
brenda
-
MMP-14 is expressed and active in cultured ES2 cells. ES2 cells also exhibit MMP-dependent invasion of and proliferation within three-dimensional collagen gels
brenda
-
the MMP-1 levels are altered in the left ventricle and serum in case of hypertrophy through hyperthyroid conditions with 3,5,3'-triiodo-L-thyroine or dexamethasone application, tissue distribution, overview
brenda
-
glycine-extended gastrin renders colon cancer cells more invasive by increasing MMP-I expression via the putative glycine-extended gastrin receptor
brenda
-
UM1 and UM2 are oral tongue squamous cell carcinoma cell lines
brenda
-
follicular expression of MMP-1 increases following the gonadotropin surge. Abundance of MMP-1 mRNA increases at 6, 12, and 48 h post-gonadotropin releasing hormone injection. MMP-1 is localized to granulosal and thecal layers of preovulatory follicles. MMP-1 is increased in bovine preovulatory follicles following the gonadotropin surge
brenda
-
enzyme expression is significantly stronger in the epithelium than in the stroma
brenda
-
the mean salivary MMP-1 concentration in patients with chronic periodontitis is significantly higher before and after treatment with aprotinin, as compared to healthy subjects
brenda
-
disruption of caveolae by addition of methyl-beta-cyclodextrin results in a dramatic decline in both motility and invasion abilities of cells with concomitant increase in secreted MMP-2 expression and expression levels of MMP-1 and MMP-9
brenda
-
disruption of caveolae by addition of methyl-beta-cyclodextrin results in a dramatic decline in both motility and invasion abilities of cells with concomitant increase in secreted MMP-2 expression and expression levels of MMP-1 and MMP-9
brenda
-
SCL-1 cell. MMP-1 is upregulated 4 h after UVA and 16 h after UVB irradiation of tumor cells. Incubation of cells with the MEK1/2 inhibitor U0126 or the p38 inhibitor SB202190 abolishes the UVA and UVB mediated induction of MMP-1
brenda
-
from Achilles tendon, immunohistochemic analysis of MMP-1, overview
brenda
-
leg ulcer tissue from patients with chronic venous insufficiency
brenda
additional information
-
MMP-1 is upregulated in the infarcted tissue compared to healthy control areas
brenda
-
of rheumatoid synovial cells stimulated with rabbit macrophage-conditioned medium
brenda
-
overexpression of phospholipid-hydroperoxide glutathione peroxidase in human dermal fibroblasts abrogates UVA irradiation-induced expression of interstitial collagenase/matrix metalloproteinase-1 by suppression of phosphatidylcholine hydroperoxide-mediated NFkappaB activation and interleukin-6 release
brenda
-
production of MMP-1 by keloid fibroblasts is 6fold greater than that of normal dermal fibroblasts. The production of MMP-1 is decreased by addition of TGF-beta1 to cultured keloid fibroblasts, while it is increased when anti-TGF-beta1 antibody is added to the culture
brenda
-
healthy dermal fibroblasts and cultured Xeroderma pigmentosum-C fibroblasts, increased MMP1 expression in cultured XP-C fibroblasts results from MMP1 mRNA accumulation and enhanced transcriptional activity of the MMP1 gene promoter, overview
brenda
-
gingival, gingival fibroblasts produce MMP-1 in response to inflammatory cytokines, such as TNF and interleukin-1
brenda
-
expression of MMP-1 is markedly increased by both onion extract and quercetin in vitro in human skin fibroblasts
brenda
-
expression of MMP-1 is markedly increased by both onion extract and quercetin in vivo in hairless mice
brenda
-
after hyperglycaemic treatment, expression of matrix metalloproteinase-1 and alpha2beta1 integrin is significantly downregulated
brenda
-
alveolar mucosa expression from HIV1+ smokers with early emphysema is significantly higher than in HIV1- smokers with early emphysema. Among the HIV- groups, compared with HIV1- healthy nonsmokers, smoking do not increase aqlveolar mucosa MMP-1 gene expression in HIV1- healthy smokers and HIV1- smokers with early emphysema, independent of whether emphysema is present or not. HIV1+ individuals with early emphysema have significantly increased expression of MMP-1 compared with all 3 groups of HIV1- individuals, including those with early emphysema
brenda
-
treatment of with 30 mM of 15-deoxy-DELTA12,14-prostaglandin J2 increases the expression of heme oxygenase-1, which precedes the induction of matrix metalloproteinases. The 15-deoxy-DELTA12,14-prostaglandin J2-induced upregulation of MMP-1 is abrogated by the heme oxygenase-1 inhibitor zinc protoporphyrin IX as well as introduction of heme oxygenase-1 short interfering RNA. Heme oxygenase-1 inducers, such as cobalt protoporphyrin IX and hemin, upregulate the expression of MMP-1. Overexpression of heme oxygenase-1 in the MCF-7 cells causes the induction of MMP-1 expression. Treatment with the heme oxygenase-1 inhibitor zinc protoporphyrin IX abolishes the migrative phenotype of 15-deoxy-DELTA12,14-prostaglandin J2-treated MCF-7 cells
brenda
-
treatment of with 30 mM of 15-deoxy-DELTA12,14-prostaglandin J2 increases the expression of heme oxygenase-1, which precedes the induction of matrix metalloproteinases. The 15-deoxy-DELTA12,14-prostaglandin J2-induced upregulation of MMP-1 is abrogated by the heme oxygenase-1 inhibitor zinc protoporphyrin IX as well as introduction of heme oxygenase-1 short interfering RNA. Heme oxygenase-1 inducers, such as cobalt protoporphyrin IX and hemin, upregulate the expression of MMP-1
brenda
-
VMM5 cells, VMM12cells and VMM39. Constitutive overexpression of collagenase 1 is mediated by the ERK pathway in invasive melanoma cells
brenda
-
expression profile of MMPs/TIMP-1 after myocardial infarction, angiotensin II receptor blockade improves MMPs/TIMP-1 balance, overview
brenda
-
collagen-induced arthritis hind paw sections as a model of human rheumatoid arthritis
brenda
-
collagen-induced arthritis hind paw sections as a model of human rheumatoid arthritis
-
brenda
-
immunohistochemic analysis of MMP-1 and TIMP-1 levels, overview. Overall plasma levels of MMP-1 and TIMP-1 in ulcerative colitis patients are significantly higher than those of the control group
brenda
-
no differences in MMP-1 in the plasma of hypertensive versus normotensive subjects
brenda
-
MMP-1 is progressively decreased from prostate intraepithelial neoplasia to prostate carcinoma
brenda
-
all-trans retinoic acid suppresses matrix metalloproteinase activity in diabetic skin
brenda
-
from mammary plastic surgery, MMP1 expression is increased in Xeroderma pigmentosum, a rare, recessively inherited genetic disease characterized by skin cancer proneness and premature aging in photoexposed area, overview
brenda
-
presence of high glucose levels and interferon gamma in culture medium have a synergistic effect on the expression of matrix metalloproteinases MMP-1, MMP-9 and interleukin-1beta. High glucose also enhances interferon gamma-induced priming effect on lipopolysaccharide-stimulated MMP-1 secretion. High glucose and interferon gamma exert the synergistic effect on MMP-1 expression by enhancing STAT1 phosphorylation and STAT1 transcriptional activity
brenda
additional information
-
overexpression of both ADAMTS1 and MMP-1 together increases osteolytic bone metastases, while overexpression of ADAMTS or MMP-1 alone has no effect
brenda
additional information
-
MMP-1 is downregulated 4fold during trophoblast differentiation, reduced MMP-1 expression in pre-eclampsia and fetal growth restriction
brenda
additional information
-
MMP-1 expression analysis in gingival tissue, overview
brenda
additional information
-
MMP-1A is strongly expressed in tumor and arthritis specimens, expression patterns of MMP-1A in a variety of healthy, cancerous and arthritic murine tissues, overview
brenda
additional information
-
MMP-1A is strongly expressed in tumor and arthritis specimens, expression patterns of MMP-1A in a variety of healthy, cancerous and arthritic murine tissues, overview
-
brenda
additional information
detection of collagen deposition and MMP-1 secretion in rat-1 fibroblasts
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
intracellular association of MMP-1 to mitochondria and nuclei confers resistance to apoptosis and may explain the association of this enzyme with tumor cell survival and spreading
brenda
-
intracellular association of MMP-1 to mitochondria and nuclei confers resistance to apoptosis and may explain the association of this enzyme with tumor cell survival and spreading
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
-
hsa-miR-222 regulates UM1 cancer cell invasion, at least in part, by indirectly regulating MMP1 expression through targeting superoxide dismutase SOD2 mRNA, overview
malfunction
-
inflammatory tissue destruction is central to pathology in cerebral tuberculosis with microglial-derived matrix metalloproteinases playing a key role in driving such damage
malfunction
-
MMP-1 is downregulated 4fold during trophoblast differentiation, reduced MMP-1 expression in pre-eclampsia and fetal growth restriction
malfunction
-
hypoxia and specifically HIF-1a increase CXCR4 and MMP1 expression in JJ cell line and chondrosarcoma invasion in vitro
malfunction
-
periodontal disease is characterized by increased expression and activity of matrix metalloproteinases and insufficient expression/activity of their inhibitors, tissue inhibitors of matrix metalloproteinases, TIMPs. This altered MMP-TIMP balance results in progressive destruction of gingival and periodontal extracellular matrix
malfunction
the catalytically domain of MMP-1 (MMP-1 CAT) alone does not cleave collagen
metabolism
-
effects of baicalin on the total protein amount and collagen I mRNA expression in periodontal ligament cells, and the regulatory effects on MMP-1/TIMP-1 expression, overview
metabolism
-
matrix metalloproteinase-1 is regulated in tuberculosis by a p38 MAPK-dependent, p-aminosalicylic acid-sensitive signaling cascade. The p38 MAPK pathway regulates the divergence between MMPs and TIMP-1, overview
metabolism
-
interleukin-6 and high glucose synergistically upregulate MMP-1 expression by U-937 cell mononuclear phagocytes via ERK1/2 and JNK pathways and c-Jun, MMP-1 regulation, overview
metabolism
-
altering the binding of at least two transcription factors, c-Jun and SP1, proteasome inhibition results in increased production of MMP-1 and decreases synthesis of type I collagen in human dermal fibroblasts. Differential effects of proteasome inhibition and TGF-beta on MMP-1 and MMP-2, overview
metabolism
the expression profiles of multiple and possibly redundant matrix-remodeling proteases (e.g., collagenases) differ strongly in health, disease, and development. Matrix metalloproteinases MMP-1 and MMP-13 cause distinct extracellular matrix (ECM) degradation, bringing about significantly distinct cellular phenotypes
metabolism
the expression profiles of multiple and possibly redundant matrix-remodeling proteases (e.g., collagenases) differ strongly in health, disease, and development. Matrix metalloproteinases MMP-1 and MMP-13 cause distinct extracellular matrix (ECM) degradation, bringing about significantly distinct cellular phenotypes
metabolism
methotrexate (MTX) significantly reduces collagen type I production in different strains of fibroblasts derived from neonatal, adult, and hypertrophic scar tissues, while under the same experimental conditions, it increases the expression of MMP-1. Possible involvement of MTX-induced extracellular signal-regulated kinase 1/2 (ERK1/2) pathway in MMP-1 production. Activation of ERK1/2 pathway plays an important role in MTX-induced MMP-1 expression in primary human dermal fibroblasts
metabolism
astragaloside IV controls collagen reduction in photoaging skin by improving transforming growth factor-beta/Smad signaling suppression and inhibiting matrix metalloproteinase-1. Transforming growth factor beta type II protein and COL1 mRNA decreased but MMP-1 and Smad7 levels increased in the photoaging model group, which is reversed by topical application of AST. AST prevents collagen reduction from UV irradiation in photoaging skin
metabolism
matrix metalloproteinase 1 and collagens play a key role in platelet-derived growth factor (PDGF) and stromal cell-derived factor-1 (SDF-1) promotion of the skin wound repairing effect of bone mesenchymal stem cells. Bone marrow mesenchymal stem cells (BMSCs) are applied to treatment of skin wounds. PDGF treatment recruits BSMCs to injured sites and strengthens the effect of BMSCs on skin wound by suppressing activity of MMP-1. SDF-1 treatment increases the treating effect of BMSCs on skin injury through the deposition of collagen I and collagen III. Phenotypes, overview
metabolism
knock-down of mitochondrial ubiquitin ligase MITOL in human dermal fibroblasts enhances the secretion of MMP-1 via interleukin-6 elicited by the activation of nuclear factor-kappaB. Knock-down of MITOL as well as UVA-irradiation increases ER stress levels. Tunicamycin, an inducer of ER stress, also increases MMP-1 secretion
metabolism
-
matrix metalloproteinase 1 and collagens play a key role in platelet-derived growth factor (PDGF) and stromal cell-derived factor-1 (SDF-1) promotion of the skin wound repairing effect of bone mesenchymal stem cells. Bone marrow mesenchymal stem cells (BMSCs) are applied to treatment of skin wounds. PDGF treatment recruits BSMCs to injured sites and strengthens the effect of BMSCs on skin wound by suppressing activity of MMP-1. SDF-1 treatment increases the treating effect of BMSCs on skin injury through the deposition of collagen I and collagen III. Phenotypes, overview
-
physiological function
-
transfection of a plasmid expression of MMP-1 into myocard after infarction increases myocyte shortening and reduces Na+-Ca2+ exchange current, it decreases myocardial fibrosis and improves cardiac remodeling and function
physiological function
-
MMP-1 is involved in in inflammatory atherosclerotic lesions and is known to be implicated in the vascular remodeling events preceding plaque rupture, the most common cause of acute myocardial infarction
physiological function
-
increased expression of MMPs by toll-like receptor activation may be involved in infection-associated inflammation, cell migration and tissue remodelling in human skin
physiological function
-
MMP-1 is increased in inflammatory conditions leading to destruction of extracellular matrix
physiological function
-
MMP-1 promotes osteoclastic bone resorption and bone metastases, the breast cancer cell produced MMP-1 is involved in the activation of the epidermal growth factor ligands that activate NF-kappaB ligand RANKL, via its central osteoclastogenic pathway receptor activator, to promote breast cancer osteolysis, molecular mechanism, overview
physiological function
-
lithium-induced MMP-1 may participate in the reinforcement of endothelial cell senescence revealing a novel mechanism for lithium-induced tissue remodeling
physiological function
-
lithium-induced MMP-1 may participate in the reinforcement of endothelial cell senescence revealing a novel mechanism for lithium-induced tissue remodeling
physiological function
-
matrix metalloproteinase-1 degrades the extracellular matrix and is implicated in tuberculosis-driven tissue destruction, signaling pathways regulating macrophage MMP-1 in human pulmonary tuberculosis, overview
physiological function
-
both plasma and mucosal levels of MMP-1 and TIMP-1 are independently correlated with ulcerative colitis, overview
physiological function
-
throughout the process of invading and remodelling spiral arteries, extracellular matrix must be broken down and matrix metalloproteinases are major participants in this disintegration
physiological function
-
matrix metalloproteinases play a pivotal role in tissue remodeling and destruction in inflammation-associated diseases such as cardiovascular disease and periodontal disease
physiological function
-
MMP-1 is implicated in the degradation of human skin matrix proteins such as collagen and other components of extracellular matrix
physiological function
-
role for MMP-1 in the TGF-beta- and EGF-stimulated collagen remodeling process
physiological function
-
MMP-1 is involved in spontaneous resorption of disc herniation after sciatica, overview. MMP-3 appears to play a greater role than MMP-1 in disc herniation resorption
physiological function
-
MMP-1 is a zinc-dependent endopeptidase capable of degrading all components of the extracellular matrix
physiological function
-
proteasome inhibition, e.g. by inhibitor bortezomib, in vitro decreases type I collagen and enhances MMP-1 production by human fibroblasts, thus favoring an antifibrotic fibroblast phenotype. These effects are dominant over the pro-fibrotic phenotype induced by transforming growth factor-beta
physiological function
-
MMP-1 or interstitial collagenase unwinds native type I collagen and initiate its degradation
physiological function
-
matrix metalloproteinases and the tissue inhibitors of MMPs, TIMPs, play a pivotal role in matrix remodeling following myocardial infarction, the MMPs/TIMP-1 balance is perturbed after myocardial infarction. Oral valsartan, but not PD123319 limits infarct size, normalized MMPs/TIMP-1 balance and restores FN level
physiological function
-
MT1-MMP is identified as the dominant and direct-acting protease responsible for the type I collagenolytic activity mediated by both mouse and human pulmonary fibroblasts. MT1-MMP is shown to be essential for pulmonary fibroblast migration within three-dimensional (3-D) hydrogels of cross-linked type I collagen that recapitulate ECM barriers encountered in the in vivo environment
physiological function
-
MT1-MMP is identified as the dominant and direct-acting protease responsible for the type I collagenolytic activity mediated by both mouse and human pulmonary fibroblasts. MT1-MMP is shown to be essential for pulmonary fibroblast migration within three-dimensional (3-D) hydrogels of cross-linked type I collagen that recapitulate ECM barriers encountered in the in vivo environment
physiological function
the protease drives morphological, biochemical, and viscoelastic changes in the extracellular matrix (ECM) leading to unique ECM-cell crosstalk, complexity and selectivity of collagenase-associated degradation mechanisms during tissue remodeling. Matrix metalloproteinases MMP-1 and MMP-13 cause distinct extracellular matrix (ECM) degradation, bringing about significantly distinct cellular phenotypes. Specific influences of the highly abundant collagenases on fibroblast-ECM crosstalk, overview
physiological function
the protease drives morphological, biochemical, and viscoelastic changes in the extracellular matrix (ECM) leading to unique ECM-cell crosstalk, complexity and selectivity of collagenase-associated degradation mechanisms during tissue remodeling. Matrix metalloproteinases MMP-1 and MMP-13 cause distinct extracellular matrix (ECM) degradation, bringing about significantly distinct cellular phenotypes. Specific influences of the highly abundant collagenases on fibroblast-ECM crosstalk, overview
physiological function
MMP-1 is one of the key regulators of the overall quantity of type I procollagen deposited by fibroblasts during scar formation. It increases collagen degradation in the extracellular matrix (ECM)
additional information
-
Rac1 signaling results in accumulation of type I collagen due to decreased collagenase activity, overview
additional information
-
c-Jun is a key subunit of AP-1 known to be essential for MMP-1 transcription
additional information
genetic variants of a common functional polymorphism in the matrix metalloproteinase-1 gene promoter do not account for the itchy skin phenotype in epidermolysis bullosa
additional information
ability of MMP-1 to unwind triple-helical collagen, collagenolytic matrix metalloproteinase structure-function relationships, molecular dynamics studies, overview. Conformational selection mechanism for collagenolysis with full-length MMPs. Dynamic crosscorrelation analysis of MMP-1 with THP, modelling. Molecular dynamics simulations are utilized to dock MMP-1 with the cleavage site region in type III collagen
additional information
although collagenolytic matrix metalloproteinases (MMPs) possess common domain organizations, there are subtle differences in their processing of collagenous triple-helical substrates
additional information
detection of collagen deposition and MMP-1 secretion in rat-1 fibroblasts, macrorheological properties and morphologies of natural and MMP-degraded ECMs
additional information
the mechanism involves the participation of an auxiliary (second) water molecule (wat2) in addition to the zinc(II)-coordinated water (wat1). The reaction initiates through a proton transfer to Glu219, followed by a nucleophilic attack by a zinc(II)-coordinated hydroxide anion nucleophile at the carbonyl carbon of the scissile bond, forming a tetrahedral intermediate. A hydrogen-bond rearrangement facilitates proton transfer from wat2 to the amide nitrogen of the scissile bond and, C-N bond cleavage takes place. The rate-determining step is the water-mediated nucleophilic attack with an activation energy barrier of 22.3 kcal/mol. The hydrogen-bond rearrangement/proton-transfer step can proceed in a consecutive or concerted manner
additional information
the critical tetrahedral intermediate is significantly stabilized through contributions from conformational flexibility and entropy. Protonation of the scissile bond nitrogen occurs via proton transfer from a Zn(II)-coordinated hydroxide rather than from a solvent water molecule. Following C-N bond cleavage, the C-terminus remains coordinated to the catalytic Zn(II), while the N-terminus forms a hydrogen bond with a solvent water molecule. Subsequently, the release of the C-terminus is facilitated by the coordination of a water molecule
Show AA Sequence and Transmembrane Helices (1316 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51929
-
x * 51929, the minor glycosylated enzyme form has a MW of 57000 Da, calculation from nucleotide sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 51929, the minor glycosylated enzyme form has a MW of 57000 Da, calculation from nucleotide sequence
additional information
-
MMP-1A comprises a signal peptide and a propeptide, a catalytic domain and a hemopexin-like domain
additional information
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MMP-1A comprises a signal peptide and a propeptide, a catalytic domain and a hemopexin-like domain
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
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the propeptide, which comprises 20% of the mass of the proenzyme, is not required for folding to a functional enzyme
proteolytic modification
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the enzyme is secreted in the form of a zymogen, proteolytic activation of procollagenase results in removal of 81 amino acid residues from the amino-terminal portion of the proenzyme
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA243-340
-
about 10% increase in turnover number and 9% increase in Km-value compared to wild-type enzyme with fTHP-3 as substrate
DELTA243-450
-
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
-
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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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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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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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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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
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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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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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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
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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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
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 60
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10 min, irreversible inactivation, little loss of activity below 50°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged isolated MMP-1A catalytic domain by nickel affinity chromatography from Escherichia coli
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solubilized and refolded recombinant enzyme by gel filtration and ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
integrity of MMP-1 promoter AP-1 binding site is necessary for transactivation by rapamycin, regulation, overview
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MMP-3/MMP-1 chimeras and variants are overexpressed in Escherichia coli, folded from inclusion bodies and isolated as zymogens
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quantitiative real-time PCR expression analysis of MMP-1 in brain regions in response to infection with Mycobacterium tuberculosis
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recombinant expression of His-tagged isolated MMP-1 catalytic domain as soluble cytoplasmic protein in Escherichia coli
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sitting drop vapor diffusion technique. Crystallization of recombinant human proMMP-1 and determination of its structure to 2.2 A resolution
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the enzyme forms insoluble inclusion bodies when over-expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activation of toll-like receptors TLR2, TLR3 or TLR5 increased the expression of MMP-1. MMP-1 and MMP-9 in human epidermal keratinocytes are induced by Pam3CSK4, Poly(I:C) and flagellin, which are ligands for TLR2, TLR3 and TLR5, respectively, overview. The induction of MMP-1 by the receptor ligands is inhibited by pretreatment with BAY11-7082, a NF-kappaB inhibitor, or SP600125, a JNK inhibitor. p38 MAPK activation negatively regulates MMP-1 induction by TLR2 or TLR5 activation, but not by TLR3 activation
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bortezomib specifically increases the steady-state mRNA levels of MMP-1 and enhances the binding of c-Jun to the promoter of MMP-1. Disruption of the proximal AP-1-binding site in the promoter of MMP-1 severely impairs MMP-1 transcription in response to bortezomib. By altering the binding of at least two transcription factors, c-Jun and SP1, proteasome inhibition results in increased production of MMP-1 and decreases synthesis of type I collagen in human dermal fibroblasts
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both the MMP-1 and TIMP-1 mRNA expression level are dramatically downregulated by baicalin
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curcumin at the concentration of 2.5-5 mg/ml specifically downregulates MMP-1 mRNA in BT-483 and MDA-MB-231 breast cancer cell lines. Cell growth and proliferation is inhibited in presence of curcumin, overview
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curcumin, a potent inhibitor for AP-1, or simvastatin inhibit the expression of MMP-1. Suppression of c-Jun expression by RNA interference significantly inhibits MMP-1 expression
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dexamethasone, and less potent also interleukin-1Ra and TNF, decrease levels of pro-MMP-1
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enhanced collagen degradation, in case of epithelial-to-mesenchymal transition stimulated by transforming growth factor-beta as well as epidermal growth factor receptor, is coupled to a significant increase in matrix metalloproteinase MMP-1 expression and is involved a proteolytic axis composed of plasmin, MMP-10, ec 3.4.24.22, and MMP-1
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expression of MMP-1 in cartilages and synovial tissues is suppressed by the treatment of curcumin and indomethacin. Production of MMP-1 is inhibited by curcumin in tumor necrosis factor-alpha-stimulated rheumatoid arthritis fibroblast-like synoviocytes and chondrocytes in a dose-dependent manner putatively through the inhibition of PKCdelta and the JNK/c-Jun signaling pathway, overview
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expression of MMP-1 is markedly increased by both onion extract and quercetin in vitro in human skin fibroblasts
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expression of MMP-1 is markedly increased by both onion extract and quercetin in vivo in hairless mice
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higenamine significantly attenuates fine-dust-induced expression of matrix metalloproteinase-1. Higenamine modulates fine-dust-induced AP-1 and NF-kappaB transactivation
hypoxia and specifically HIF-1a increase CXCR4, its ligand SDF1, and MMP1 expressions in JJ cell line and chondrosarcoma invasion in vitro, which can be inhibited by siRNA directed at HIF-1a or CXCR4, the CXCR4 inhibitor AMD3100, as well as with ERK inhibitor U0126 and ERK siRNA. Hypoxia increases MMP1 mRNA expression 9fold which is further increased to 23fold by SDF1 stimulation
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ibuprofen upregulates expressions of matrix metalloproteinase-1, as well as MMP-8, MMP-9, and MMP-13, without affecting expressions of types I and III collagen in tendon cells
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increased MMP1 expression in JJ cell line can be inhibited by siRNA directed at HIF-1a or CXCR4, the CXCR4 inhibitor AMD3100, as well as with ERK inhibitor U0126 and ERK siRNA
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induction of MMP-1 by UV-A irradiation treatment of cultured human dermal fibroblasts
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inhibititory effects of potent antioxidant astaxanthin on the MMP-1 induction by UV-A irradiation, overview
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interleukin-6, high glucose, and lipopolysaccharide act in concert and synergistically upregulate MMP-1 expression by U-937 mononuclear phagocytes via ERK1/2 and JNK pathways and c-Jun, mechanism, overview. c-Jun is a key subunit of AP-1 known to be essential for MMP-1 transcription
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lithium specifically induces a rapid and pronounced up-regulation of MMP-1 at the mRNA and protein levels, whereas the induction of two the other senescent cell markers plasminogen activator inhibitor-1 and interleukin-8 is either delayed or weak, respectively. Lithium affects MMP-1 expression mainly at the transcriptional level but neither the AP1/Ets regulatory sites nor the redox sensitive -1607/2G site in MMP-1 promoter are involved in lithium-dependent MMP-1 regulation
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matrix metalloproteinase-1 expression is induced by interleukin-1beta requiring acid sphingomyelinase, overview
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methotrexate (MTX) increases the expression of MMP-1 in primary human neonatal, adult, and hypertrophic scar fibroblasts by 1.5fold 72 h after treatment with 50-500 ng/ml MTX
MMP-1 expression and secretion is induced by infection with Mycobacterium tuberculosis by 57.8%, the specific inhibitor TIMP-1 expression is also induced by 243.7%. The MMP-1 induction is specifically inhibited by 4-aminosalicyclic acid via inhibiting a p38 MAPK-prostaglandin signaling cascade, overview
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MMP-1 expression is induced by UV-B irradiation, the induction is inhibited by extracts of Kaempferia pandurata, as are phosphorylation of MAP kinases ERK, JNK, and p38, overview
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MMP-1 is 4.1fold induced by infection with Mycobacterium tuberculosis. Conditioned medium from Mycobacterium tuberculosis-infected human monocytes stimulates greater MMP-1 gene expression in human microglial cells than direct infection, overview. The induction is suppressed by dexamethasone. TNF-alpha and interleukin-1beta are necessary but not sufficient for upregulating MMP-1 secretion. NF-kappaB and AP-1 c-Jun/FosB heterodimers regulate induction of MMP-1 secretion by conditioned medium from Mycobacterium tuberculosis and are upregulated in granulomas from patients with cerebral tuberculosis. CoMTb upregulates MMP-1 gene expression and secretion in microglia
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MMP-1 is downregulated 4fold during trophoblast differentiation, reduced MMP-1 expression in pre-eclampsia and fetal growth restriction
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MMP-1 is induced in gingival fibroblasts in response to inflammatory cytokines, such as TNF and interleukin-1. TNF treatment of human gingival fibroblasts significantly induces the expression of MMP-1 severalfold, while enamel matrix derivative alone has no effect
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MMP-1 is upregulated after stroke in brain in the infarcted tissue compared to healthy control areas, overview
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phorbol 12-myristate 13-acetate and interleukin-1beta significantly stimulate the production of MMP-1 by periodontal ligament cells at both the transcriptional and the translational level
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production of MMP-1 is inhibited by curcumin in collagen-induced arthritis hind paw sections in a dose-dependent manner putatively through the inhibition of PKCdelta and the JNK/c-Jun signaling pathway, overview
Rac1 inhibitor NSC23766 suppresses MMP1 in dermal fibroblasts, and half-lives of type I collagen protein are increased
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recombinantly overexpressed RhoB enhances migration and MMP1 expression of prostate cancer DU145 cells, overview
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TNF-alpha and IL-1beta stimulate production of MMPs through the activation of mitogen-activated protein kinases, NF-kappaB and AP-1
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transforming growth factor TGF-beta1 downregulates the expression and production of MMP1 via a TbetaRII/ALK5-mediated SMAD-dependent signaling pathway in human granulosa-lutein cells. This is mediated by transcription factor, the inhibitor of differentiation 3 (ID3) protein
transglutaminase TG2 mediates dsRNA-induced MMP-1 expression through NF-kappaB activation. TG2 activity enhances translocation of p65 into the nucleus, where it augments transcription of MMP
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treatment with quercetin dose-dependently suppresses poly(I:C)-induced MMP expression. Ex vivo cultured skin from Tgm2-/- mice exhibits a significantly reduced level of MMP mRNA compared with those from wild-type mice
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UV-B irradiation induces MMP-1 expression and secretion. Inhibitory effects of Costaria costata fucoidan on UVB-induced MMP-1 promoter, mRNA, and protein expression in vitro by 41.8% at 10 ng/ml, 57.7% at 100 ng/ml, and 70% at 0.001 mg/ml compared to UV-B irradiation alone, overview
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UVA and UVB irradiation of dermal fibroblasts in vitro or human skin in vivo induces MMP-1 expression. MMP-1 expression and secretion induced by UV-B irradiation is inhibited by trans-zeatin, a cytokinin from Zea mays, and by PD98059, an ERK inhibitor, by SP600125, a JNK inhibitor and by SB203580, a p38 MAPK inhibitor. trans-Zeatin also inhibits UVB-induced ERK, JNK, p38 MAPK and c-Jun phosphorylation
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production of MMP-1 is inhibited by curcumin in collagen-induced arthritis hind paw sections in a dose-dependent manner putatively through the inhibition of PKCdelta and the JNK/c-Jun signaling pathway, overview
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production of MMP-1 is inhibited by curcumin in collagen-induced arthritis hind paw sections in a dose-dependent manner putatively through the inhibition of PKCdelta and the JNK/c-Jun signaling pathway, overview
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
optimal folding occurs when the denatured protein is diluted at 4°C in 2 M guanidine HCl, 20% glycerol, 2.5 mM reduced and oxidized glutathione, 5 mM CaCl2, followed by buffer exchange to remove denaturant and thiols
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recombinant enzyme from inclusion bodies is solubilized in denaturation buffer containing 50 mM Tris, pH 8.0, 20 mM DTT, 50 mM ZnCl2, 1 mM acetohydroxamic acid (AHA), and 8 M urea, stirred overnight at room temperature, followed by ultrafiltration and anion exchange chromatography. The enzyme is diluted in 20 mM Tris, pH 8.0, 20 mM cystamine, 6 M urea, and dialyzed against 5-8 l of 50 mM Tris, pH 8.0, 2 mM AHA, 1 mM hydroxyethyl sulfate, 4 M urea, 5 mM CaCl2 , 0.1 mM ZnCl2, 300 mM NaCl, 5 mM 2-mercaptoethanol, and 4 M urea at 4°C overnight with stirring. The last step of refolding is done twice, against 2 M urea, 50 mM Tris, pH 8.0, 10 mM CaCl2, 0.1 mM ZnCl2, 300 mM NaCl, and 2 mM AHA overnight, with stirring, at 4°C
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
diagnostics
drug development
MMP-1 enzyme inhibitor astragaloside IV is a potential agent against skin photoaging
medicine
synthesis
improved method for high-level expression of soluble human MMP-1 catalytic domain in Escherichia coli
analysis
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detection of localized extracellular sites of protease activity by use of fluorescent biosensor rhodamine 6G-labeled KDP-6-aminohexanoic acid-GPLGIAGIG-6-aminohexanoic acid-PKGY. Protease activity is localized at the polarized leading edge of migrating tumor cells rather than further back on the cell body. The path of proteolytic cleavage by a migrating cell can be visualized in 2- and 3-dimensional matrices. Probe can be used to determine inhibitor concentrations needed to suppress cell-surface protease activity
analysis
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generation of specific recombinant human monoclonal antibody SP1, which may serve as building block for the development of antibody-based therapy strategies in mouse models of pathology
analysis
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generation of specific recombinant human monoclonal antibody SP1, which may serve as building block for the development of antibody-based therapy strategies in mouse models of pathology
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diagnostics
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MMP1 is a potential oral cancer marker in gingiva, but not in neck tissue
medicine
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glycine-extended gastrin renders colon cancer cells more invasive by increasing MMP-I expression via the putative glycine-extended gastrin receptor and would thus be a good molecular target in a clinical setting
medicine
MMP-8, MMP-9, and to a lesser extent, MMP-2, MMP-3, MMP-11 and MMP-12 are present at higher levels in lung secretions of pediatric acute lung injury patients compared with controls. Almost all MMP-8 detected at later disease course is constitutively active, while in subjects who remain intubated for >10 days, MMP-9 activity decreases
medicine
-
protease activity is localized at the polarized leading edge of migrating tumor cells rather than further back on the cell body. Activity is essential for cell migration in native cross-linked but not pepsin-treated collagen matrices
medicine
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in leg ulcer tissue from patients with chronic venous insufficiency, matrix metalloproteinases MMP-1, MMP-2, MMP-3, MMP-8, MMP-9, MMP-12, and MMP-13 protein levels are elevated. Following compression therapy, reduction of MMP-1, MMP-2, and MMP-3 levels is associated with significantly higher rates of ulcer healing at 4 weeks
medicine
-
in tear samples of vernal keratoconjunctivitis patients, matrix metalloproteinase-1, matrix metalloproteinase-2, matrix metalloproteinase-3, matrix metalloproteinase-9 and matrix metalloproteinase-10 are highly present in all samples
medicine
-
investigation on the relation of serum matrix metalloprotease MMP-1 and vascular endothelial growth factor VEGF-A concentrations to cardiac allograft rejection. Mean week 1 and week 2 serum MMP-1 concentrations predict rejection. At the optimal cutoff level of >7.5 ng/ml, MMP-1 predicts rejection with 82% sensitivity and 72% specificity. Initial serum MMP-1 <5.3 ng/ml is associated with rejection-free outcome in 80% of patients. Both MMP-1 and VEGF-A predict rejection on the next endomyocardial biopsies, while rejection at endomyocardial biopsy is identified only by VEGF-A. Patients receiving combined cyclosporine-A and everolimus have the lowest serum MMP-1 concentrations. While serum MMP-1 predicts rejection-free outcome and VEGF-A identifies rejection on endomyocardial biopsy, both markers predict rejection in follow-up of cardiac transplant recipients
medicine
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in ovariectomized rats, during the first 1-4 weeks there is a significant increase in collagen accumulation and an increase MT1-MMP expression. Although active-form matrix metalloproteinase MMP-2 and collagen progressively return to normal levels, the markedly increased collagen deposition appears again at 8 weeks and persists until 12 weeks, followed by induction of MMP-2 and MT1-MMP at 12 weeks
medicine
-
high level expression of MMP-14 and MMP-2 are observed in ovarian clear cell carcinoma relative to other histotypes
medicine
-
patients who underwent direct current electrical cardioversion for persistent atrial fibrillation have increased levels of C-reactive protein and lower levels of MMP-1 compared with controls. There are no differences in baseline levels of C-reactive protein, MMP-1, TIMP-1 and carboxyterminal telopeptide of collagen type I between those where electrical cardioversion was unsuccessful, compared to those with immediate EC success. Patients who maintain sinus rhythm at 30 days' follow-up have lower levels of C-reactive protein
medicine
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MMP-1 suppressor Costaria costata fucoidan is a potential therapeutic agent for the prevention and treatment of photoaging of the skin
medicine
MMP-1-mediated fragmentation of dermal collagen fibrils alters the morphology and function of dermal fibroblasts, linking collagen fibril fragmentation to age-related decline of fibroblast function
medicine
higenamine significantly attenuates fine-dust-induced expression of matrix metalloproteinase-1. Higenamine modulates fine-dust-induced AP-1 and NF-kappaB transactivation
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