Information on EC 3.4.24.7 - interstitial collagenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.4.24.7
-
RECOMMENDED NAME
GeneOntology No.
interstitial collagenase
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
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
azocollase
-
-
-
-
collagen peptidase
-
-
-
-
collagen protease
-
-
-
-
collagen protease
-
-
collagenase
-
-
-
-
collagenase
-
-
collagenase 1
-
-
collagenase A
-
-
-
-
collagenase MMP-1
-
-
-
-
collagenase-1
-
-
collagenase-1
-
-
EC 3.4.99.5
-
-
related
-
ect-MMP-14
-
ectodomain
Fibroblast collagenase
-
-
-
-
HSFC
-
-
kollaza
-
-
-
-
macrophage matrix metalloproteinase
-
-
matrix metalloproteinase 1
-
-
-
-
matrix metalloproteinase 1
-
-
matrix metalloproteinase 1
-
-
matrix metalloproteinase 1
Mus musculus Sv129
-
-
-
matrix metalloproteinase-1
-
-
-
-
matrix metalloproteinase-1
-
-
matrix metalloproteinase-1
-
-
matrix metalloproteinase-1
P03956
-
matrix metalloproteinase-1
-
-
matrix metalloproteinase-1
Mus musculus DBA/1J
-
-
-
matrix metalloproteinase-1
-
-
matrix metalloproteinase-18
-
-
-
-
matrix-metalloproteinase-1
-
-
membrane-type 1-MMP
-
-
metallocollagenase
-
-
-
-
metalloproteinase-1
-
-
-
-
MMP-1
-
-
-
-
MMP-1
P03956
-
MMP-1
Mus musculus DBA/1J
-
-
-
MMP-12
-
-
MMP-14
-
-
MMP-1A
-
-
MMP-1A
Mus musculus Sv129
-
-
-
MT1-MMP
-
-
Myocardial collagenase
-
-
-
-
nucleolysin
-
-
-
-
soycollagestin
-
-
-
-
TC1
-
-
-
-
tumor collagenase
-
-
vertebrate collagenase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9001-12-1
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Frog
-
-
-
Manually annotated by BRENDA team
DNA repair-deficient/cancer-prone xeroderma pigmentosum group C patients, Caucasian and Black
-
-
Manually annotated by BRENDA team
HSFC
-
-
Manually annotated by BRENDA team
patients with atrial fibrillation
-
-
Manually annotated by BRENDA team
patients with chronic venous insufficiency
-
-
Manually annotated by BRENDA team
patients with pediatric acute lung injury
UniProt
Manually annotated by BRENDA team
patients with primary epithelial ovarian tumors
-
-
Manually annotated by BRENDA team
recipients of heart transplantation
-
-
Manually annotated by BRENDA team
vernal keratoconjunctivitis patients
-
-
Manually annotated by BRENDA team
DBA/1J mice
-
-
Manually annotated by BRENDA team
Sv129 mice
-
-
Manually annotated by BRENDA team
Mus musculus DBA/1J
DBA/1J mice
-
-
Manually annotated by BRENDA team
Mus musculus Sv129
Sv129 mice
-
-
Manually annotated by BRENDA team
male Lewis rats
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
hypoxia and specifically HIF-1a increase CXCR4 and MMP1 expression in JJ cell line and chondrosarcoma invasion in vitro
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
-
MMP-1 is involved in photoaging of the skin
malfunction
-
MMP-1A is strongly expressed in tumor and arthritis specimens
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
Mus musculus Sv129
-
MMP-1A is strongly expressed in tumor and arthritis specimens
-
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
-
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
-
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
physiological function
-
both plasma and mucosal levels of MMP-1 and TIMP-1 are independently correlated with ulcerative colitis, overview
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
-
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
-
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
-
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 a zinc-dependent endopeptidase capable of degrading all components of the extracellular matrix
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
-
MMP-1 is increased in inflammatory conditions leading to destruction of extracellular matrix
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
-
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 or interstitial collagenase unwinds native type I collagen and initiate its degradation
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
-
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
-
role for MMP-1 in the TGF-beta- and EGF-stimulated collagen remodeling process
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
-
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
-
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
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
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
-
Rac1 signaling results in accumulation of type I collagen due to decreased collagenase activity, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
-
-
-
-
?
(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
show the reaction diagram
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-cyclohexylalanine-Gly-Nve-His-Ala-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-NH2 + H2O
?
show the reaction diagram
-
degradation of synthetic substrate is pH-independent
-
-
?
2,4-dinitrophenyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-NH2 + H2O
?
show the reaction diagram
Frog
-
-
-
-
?
Ac-Pro-Leu-Gly-SCH2(iBu)CO-Leu-Leu-GlyOEt + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Pro-Ala-Gly-Ile-Ala-Gly-Gln-Arg-ethyl ester + H2O
acetyl-Pro-Ala-Gly + Ile-Ala-Gly-Gln-Arg-ethyl ester
show the reaction diagram
Frog
-
-
-
?
acetyl-Pro-Gln-Gly-Ile-Ala-Gly-ethyl ester + H2O
acetyl-Pro-Gln-Gly + Ile-Ala-Gly-ethyl ester
show the reaction diagram
Frog
-
-
-
?
acetyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Arg-ethyl ester + H2O
acetyl-Pro-Gln-Gly + Ile-Ala-Gly-Gln-Arg-ethyl ester + H2O
show the reaction diagram
Frog
-
-
-
?
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
show the reaction diagram
Frog
-
-
-
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
show the reaction diagram
-
-
-
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
show the reaction diagram
-
-
-
-
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
show the reaction diagram
-
-
-
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
show the reaction diagram
-
very low activity
-
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
show the reaction diagram
-
-
-
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-OC2H5 + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Pro-Leu-Gly-Leu-Ala-Gly-OC2H5 + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
show the reaction diagram
-
-
-
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-OC2H5 + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
show the reaction diagram
-
-
-
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
show the reaction diagram
-
very low activity
-
?
acetyl-Pro-Leu-Gly-S-Leu-Leu-Gly ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Pro-Leu-Gly-SCH2[CH2CH(CH3)2CO]-Leu-Leu-OC2H5 + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
show the reaction diagram
-
-
-
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
show the reaction diagram
-
very low activity
-
?
alpha1(I)772-786 triple-helical peptide + H2O
?
show the reaction diagram
-
-
-
-
?
butyloxycarbonyl-Pro-Ala-Gly-Ile-Ala-Gly-ethyl ester + H2O
butyloxycarbonyl-Pro-Ala-Gly + Ile-Ala-Gly-ethyl ester
show the reaction diagram
Frog
-
-
-
?
butyloxycarbonyl-Pro-Gln-Gly-Ile-Ala-Gly-ethyl ester + H2O
butyloxycarbonyl-Pro-Gln-Gly + Ile-Ala-Gly-ethyl ester
show the reaction diagram
Frog
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
casein zymography assay method
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
Frog
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
P03956
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
two collagen fragments representing 77% and 23% respectively of the length of the collagen molecule
?
Collagen + H2O
?
show the reaction diagram
-
native reconstituted guinea pig skin collagen fibrils
-
-
?
Collagen + H2O
?
show the reaction diagram
-
rat tendon type I collagen
-
-
?
Collagen + H2O
?
show the reaction diagram
-
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
-
-
?
Collagen + H2O
?
show the reaction diagram
-
native calf skin collagen
-
-
?
Collagen + H2O
?
show the reaction diagram
-
type X collagen, two cleavage sites, three products with 32000 Da, 18000 Da and 9000 Da chains
-
-
?
Collagen + H2O
?
show the reaction diagram
-
below 30C 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 37C and neutral pH, the enzyme degrades native collagen fibrils or molecules to peptides most of which are dialyzable
-
-
?
Collagen + H2O
?
show the reaction diagram
-
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
-
-
?
Collagen + H2O
?
show the reaction diagram
-
type I collagen
-
-
?
collagen I + H2O
?
show the reaction diagram
-
degradation
-
-
?
collagen I + H2O
?
show the reaction diagram
-
degradation
-
-
?
collagen I + H2O
?
show the reaction diagram
-
degradation, calf skin substrate
-
-
?
collagen I alpha-1 chain + H2O
?
show the reaction diagram
-
MMP-14 ectodomain preferentially cleaves the alpha-1 chain, the overall enzymatic activity is higher on the alpha-2 chain for MMP-1 and MMP-2
-
-
?
collagen I alpha-2 chain + H2O
?
show the reaction diagram
-
MMP-14 ectodomain preferentially cleaves the alpha-1 chain, the overall enzymatic activity is higher on the alpha-2 chain for MMP-1 and MMP-2
-
-
?
GAQGIAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
GLQGIAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Ala-Gly-Gln-Gln
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
GNQGIAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
GNVGLAGA + H2O
?
show the reaction diagram
-
-
-
-
?
GP-Hyp-GIAGA + H2O
?
show the reaction diagram
-
-
-
-
?
GP-Hyp-IAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
GPDGIAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
GPLGIAGP + H2O
?
show the reaction diagram
-
-
-
-
?
GPLGIAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
GPQGIAGA + H2O
?
show the reaction diagram
-
-
-
-
?
GPQGIAGH + H2O
?
show the reaction diagram
-
-
-
-
?
GPQGIAGP + H2O
?
show the reaction diagram
-
-
-
-
?
GPQGIAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
GPQGIAGT + H2O
?
show the reaction diagram
-
-
-
-
?
GPQGLAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
GPRGIAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
GPVGIAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
Human alpha2-macroglobulin + H2O
?
show the reaction diagram
-
cleavage site: Gly679-Leu680
-
-
?
human pregnancy zone protein + H2O
?
show the reaction diagram
-
cleavage sites: Gly685-Leu686, Gly687-Val688, Gly757-Ile758, Ala684-Leu684, and Ala685-Met686
-
-
?
Pro-Gln-Gly-Ile-Ala-Gly-Gln-Arg-ethyl ester + H2O
Pro-Gln-Gly + Ile-Ala-Gly-Gln-Arg-ethyl ester
show the reaction diagram
Frog
-
-
-
?
PSYFLNAG + H2O
?
show the reaction diagram
-
-
-
-
?
rat alpha1 macroglobulin + H2O
?
show the reaction diagram
-
cleavage site: His681-Leu682, Phe691-Leu692
-
-
?
rat alpha1-inhibitor 3 (27J) + H2O
?
show the reaction diagram
-
cleavage sites: Ala666-Val667
-
-
?
rat alpha1-inhibitor 3 (2J) + H2O
?
show the reaction diagram
-
cleavage sites: Pro683-Val684
-
-
?
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
show the reaction diagram
-
fluorescent biosensor, substrate for matrix metalloproteinases MMP-2, MMP-9, MMP-14
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
a plasmin/MMP-10/MMP-1 proteolytic axis effectively enhances collagen type 1 degradation
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
interstitial collagen
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
production of type I collagen by periodontal ligament cells
-
-
?
type I procollagen + H2O
type I collagen + ?
show the reaction diagram
-
-
-
-
?
type II collagen + H2O
?
show the reaction diagram
-
interstitial collagen
-
-
?
type III collagen + H2O
?
show the reaction diagram
-
-
-
-
?
type III collagen + H2O
?
show the reaction diagram
-
interstitial collagen
-
-
?
type III collagen + H2O
?
show the reaction diagram
-
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
-
-
?
[alpha1(I)]2alpha2(I)772-784 triple-helical peptide + H2O
?
show the reaction diagram
-
-
-
-
?
[alpha1(II)769-783] fluorogenic triple-helical peptide-3 + H2O
?
show the reaction diagram
-
-
-
-
?
[alpha1(II)769-783] fluorogenic triple-helical peptide-4 + H2O
?
show the reaction diagram
-
-
-
-
?
[alpha1(II)769-783] single-stranded peptide-3 + H2O
?
show the reaction diagram
-
-
-
-
?
collagen III + H2O
?
show the reaction diagram
-
degradation
-
-
?
fTHP-3 + H2O
additional information
-
-
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
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
-
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
show the reaction diagram
Mus musculus, Mus musculus Sv129
-
fluorogenic substrate
-
-
?
additional information
?
-
-
relative rates of hydrolysis in decreasing order: GPQGIAGQ, PSYFLNAG, GNVGLAGA
-
-
-
additional information
?
-
-
the enzyme prefers very lipophilic sequences
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
MMP-1 is involved in intestinal re-epithelization in vivo and is upregulated by cytokines relevant in wound repair
-
-
-
additional information
?
-
-
enzyme regulation on expression and protein levels, overview
-
-
-
additional information
?
-
-
MMP-1 is a single effector of the Raf/MEK/ERK signaling cascade, that prevents progression of melanoma from a primary to metastatic tumor
-
-
-
additional information
?
-
-
MMP1 expression is increased in Xeroderma pigmentosum, a rare, recessively inherited genetic disease characterized by skin cancer proneness and premature aging in photoexposed area
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
substance P up-regulates matrix metalloproteinase-1 and down-regulates collagen in human lung fibroblast, overview
-
-
-
additional information
?
-
-
active MMP-10, EC 3.4.24.22, does not cleave collagen type 1 directly, it does activate the collagenase MMP-1
-
-
-
additional information
?
-
-
matrix metalloproteinases are endopeptidases capable of cleaving various components of extracellular matrix
-
-
-
additional information
?
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
collagen I + H2O
?
show the reaction diagram
-
degradation
-
-
?
collagen I + H2O
?
show the reaction diagram
-
degradation
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
a plasmin/MMP-10/MMP-1 proteolytic axis effectively enhances collagen type 1 degradation
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
interstitial collagen
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
production of type I collagen by periodontal ligament cells
-
-
?
type I procollagen + H2O
type I collagen + ?
show the reaction diagram
-
-
-
-
?
type II collagen + H2O
?
show the reaction diagram
-
interstitial collagen
-
-
?
type III collagen + H2O
?
show the reaction diagram
-
-
-
-
?
type III collagen + H2O
?
show the reaction diagram
-
interstitial collagen
-
-
?
collagen III + H2O
?
show the reaction diagram
-
degradation
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
MMP-1 is involved in intestinal re-epithelization in vivo and is upregulated by cytokines relevant in wound repair
-
-
-
additional information
?
-
-
enzyme regulation on expression and protein levels, overview
-
-
-
additional information
?
-
-
MMP-1 is a single effector of the Raf/MEK/ERK signaling cascade, that prevents progression of melanoma from a primary to metastatic tumor
-
-
-
additional information
?
-
-
MMP1 expression is increased in Xeroderma pigmentosum, a rare, recessively inherited genetic disease characterized by skin cancer proneness and premature aging in photoexposed area
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
substance P up-regulates matrix metalloproteinase-1 and down-regulates collagen in human lung fibroblast, overview
-
-
-
additional information
?
-
-
active MMP-10, EC 3.4.24.22, does not cleave collagen type 1 directly, it does activate the collagenase MMP-1
-
-
-
additional information
?
-
-
matrix metalloproteinases are endopeptidases capable of cleaving various components of extracellular matrix
-
-
-
additional information
?
-
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
-
Ca2+
-
required
Ca2+
-
both collagen and globular protein substrates of collagenase may bind Ca2+ and Zn2+ in the active site
Zn2+
-
a zinc-containing endopeptidase
Zn2+
-
required
Zn2+
-
required for activity
Zn2+
-
both collagen and globular protein substrates of collagenase may bind Ca2+ and Zn2+ in the active site
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-phenyl)-carbamic acid tert-butyl ester
-
-
1,10-phenanthroline
-
chelates the required Zn2+
1,10-phenanthroline
-
-
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-[(2-Hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-benzoic acid
-
-
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-Bromo-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-(3-Chloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-(4-Chloro-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-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-(4-Fluoro-phenylsulfonyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-Benzoyl-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[Benzenesulfonyl-(4-nitro-benzyl)-amino]-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
-
-
-
4-[(2-Hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-benzoic acid
-
-
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
alpha2-Macroglobulin
-
-
-
batimastat
-
i.e. BB-94
benzo[a]pyrene
P81563
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, 25C, pH 7.4, Tris buffer, strong irreversible inhibition, inhibition increases with higher temperatures and inhibitor concentration
ClCH2CO-(N-OH)Phe-Ala-Ala-NH2
-
-
CT 1746
-
-
-
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
dithiothreitol
-
-
EDTA
-
-
epigallocatechin-3-gallate
-
-
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
-
GM6001
-
a broad-spectrum MMP inhibitor
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
HSCH(CH2C6H5)CO-Ala-Gly-Gln-D-Arg-NH2
Frog
-
-
-
HSCH(CH2CH(CH3)2)CO -Ala-Gly-Gln-D-Arg-NH2
Frog
-
-
-
HSCH2CH(NH2)CO-Ala-Gly-Gln-D-Arg-NH2
Frog
-
-
-
marimastat
-
i.e. BB-2516
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-[(2-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(3-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-iodo-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-methoxy-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-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)-(2-nitro-phenylsulfanyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(3-trifluoromethyl-benzenesulfonyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(4-nitro-phenylsulfanyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(nonachlorobutane-1-sulfonyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(quinoline-8-sulfonyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(toluene-4-sulfonyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-pentafluorobenzenesulfonyl-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-phenylmethanesulfonyl-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-trichloromethanesulfonyl-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-trifluoromethanesulfonyl-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-Hydroxy-3-[(naphthalene-1-sulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(naphthalene-2-sulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[1-(4-nitro-benzyl)-3-o-tolylsulfonyl-ureido]-propionamide
-
-
N-Hydroxy-3-[1-(4-nitro-benzyl)-3-p-tolylsulfonyl-ureido]-propionamide
-
-
N-Hydroxy-3-[1-(4-nitro-benzyl)-3-phenylsulfonyl-ureido]-propionamide
-
-
N-Hydroxy-3-[dimethylsulfamoyl-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[methanesulfonyl-(4-nitro-benzyl)-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
-
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 M, 25C, 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
Ro-31-9790
-
-
Serum
-
-
-
TIMP-1
-
expression profile of MMPs/TIMP-1 after myocardial infarction, angiotensin II receptor blockade improves MMPs/TIMP-1 balance, overview
-
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
-
determination in cell culture medium
-
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-2
-
-
-
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
-
TIMP-2
-
determination in cell culture medium
-
TIMP-2
-
highly produced in brain microvessels
-
TIMP-3
-
is induced by enamel matrix derivative
-
tissue inhibitor of matrix metalloproteinase-1
-
is not influenced by substance P
-
tissue inhibitor of matrix metalloproteinase-1
-
-
-
tissue inhibitor of matrix metalloproteinase-2
-
0.1 microM, inhibits both protease activity and migration in a 3-dimensional cross-linked collagen matrix
-
Tissue inhibitor of metalloproteinase-1
-
TIMP-1
-
tissue inhibitors of metalloproteinase-1
-
i.e. TIMP-1
-
trocade
-
i.e. RO-22-3555
TVGCEECTV
-
-
[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
-
-
-
mercaptophenylalanyl derivatives
Frog
-
-
-
additional information
-
human tissue factor pathway inhibitor-2 does not bind or inhibit activated matrix metalloproteinase-1
-
additional information
-
sulfur based inhibitors
-
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
-
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
-
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
-
TNF
-
increases active MMP-1 level
-
Trypsin
-
procollagenase activated to collagenase
-
interleukin-1 receptor antagonist
-
increases active MMP-1 level
-
additional information
-
essential role of activator protein-1 activation in constitutive MMP1 overexpression in Xeroderma pigmentosum-C primary fibroblasts
-
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
-
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
-
dexamethasone induces myocardial matrix degradation by MMP-1
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0013
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-OC2H5
-
-
0.0012
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-OC2H5
-
-
0.0039
acetyl-Pro-Leu-Gly-SCH[CH2CH(CH3)2CO]-Leu-Leu-OC2H5
-
-
-
0.063
alpha1(I)772-786 triple-helical peptide
-
wild-type enzyme
-
0.2076
alpha1(I)772-786 triple-helical peptide
-
mutant enzyme DELTA243-450
-
0.0002
bovine type I collagen
-
-
-
0.00000000086
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 1-protonated
-
0.0000000011
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 1-protonated
-
0.0000000075
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 0-protonated
-
0.000000016
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 2-protonated
-
0.000000045
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 0-protonated
-
0.00000012
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 3-protonated
-
0.00000017
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 2-protonated
-
0.00000074
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 3-protonated
-
0.00000000025
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 1-protonated
-
0.0000000024
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 2-protonated
-
0.0000000028
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 1-protonated
-
0.000000004
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 2-protonated
-
0.000000011
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 0-protonated
-
0.00000014
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 3-protonated
-
0.00000046
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 3-protonated
-
0.00000053
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 0-protonated
-
0.0612
fTHP-3
-
30C, MMP-1
-
0.0666
fTHP-3
-
30C, MMP-1(DELTA243-450)
-
3.3
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Gln
-
wild-type enzyme
0.63
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Gln-Arg-Gly-Val-Val-Gly-Leu-Hyp-NH2
-
wild-type enzyme
3.6
GPLGIAGQ
-
-
3.6
GPQGIAGA
-
-
3.3
GPQGIAGQ
-
-
2.4
GPQGIAGT
-
-
2.8
GPQGLAGQ
-
-
5.6
GPRGIAGQ
-
-
4.9
GPVGIAGQ
-
-
0.0005
human type I collagen
-
-
-
0.0008
human type I collagen
-
-
-
0.0009
human type I collagen
-
-
-
0.0011
human type I collagen
-
-
-
0.001
human type II collagen
-
-
-
0.0021
human type II collagen
-
-
-
0.0013
human type III collagen
-
-
-
0.0017
human type III collagen
-
-
-
0.8
type I collagen
-
-
-
0.0013
type III collagen
-
pH 7.5, 25C, wild-type substrate
-
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
-
0.171
[alpha1(II)769-783] single-stranded peptide-3
-
wild-type enzyme
-
0.0024
human type III collagen
-
-
-
additional information
additional information
-
kinetics with wild-type and mutant FG-5015 I785P type III collagen substrates, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.3
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-OC2H5
-
-
5.83
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-OC2H5
-
-
103
acetyl-Pro-Leu-Gly-SCH[CH2CH(CH3)2CO]-Leu-Leu-OC2H5
-
-
-
0.11
alpha1(I)772-786 triple-helical peptide
-
wild-type enzyme
-
0.28
alpha1(I)772-786 triple-helical peptide
-
mutant enzyme DELTA243-450
-
0.00147
bovine type I collagen
-
-
-
0.21
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 0-protonated
-
0.3
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 1-protonated
-
0.43
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 2-protonated
-
0.65
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 3-protonated
-
0.66
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 1-protonated
-
1.83
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 2-protonated
-
4.56
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 0-protonated
-
10.41
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 3-protonated
-
0.014
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 2-protonated
-
0.089
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 1-protonated
-
0.54
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 3-protonated
-
0.79
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 2-protonated
-
4.09
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 3-protonated
-
5.44
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 1-protonated
-
16.9
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 0-protonated
-
58.61
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 0-protonated
-
0.08
fTHP-3
-
30C, MMP-1
-
0.087
fTHP-3
-
30C, MMP-1(DELTA243-450)
-
0.2
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Gln
-
wild-type enzyme
0.51
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Gln-Arg-Gly-Val-Val-Gly-Leu-Hyp-NH2
-
wild-type enzyme
0.333
GPLGIAGQ
-
-
0.217
GPQGIAGA
-
-
0.203
GPQGIAGQ
-
-
0.263
GPQGIAGT
-
-
0.27
GPQGLAGQ
-
-
0.0717
GPRGIAGQ
-
-
0.15
GPVGIAGQ
-
-
0.0035
human type I collagen
-
-
-
0.00375
human type I collagen
-
-
-
0.0148
human type I collagen
-
-
-
0.000267
human type II collagen
-
-
-
0.000383
human type II collagen
-
-
-
0.00392
human type II collagen
-
-
-
0.0056
human type III collagen
-
-
-
0.0958
human type III collagen
-
-
-
0.153
human type III collagen
-
-
-
0.00278
type I collagen
-
-
-
0.077
type III collagen
-
pH 7.5, 25C, wild-type substrate
-
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
-
0.25
[alpha1(II)769-783] single-stranded peptide-3
-
wild-type enzyme
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
880000
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 3-protonated
0
2500000
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 2-protonated
0
28000000
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 0-protonated
0
88000000
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 3-protonated
0
100000000
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 0-protonated
0
120000000
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 2-protonated
0
360000000
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 1-protonated
0
630000000
collagen I alpha-1 chain
-
pH not specified in the publication, 37C, MMP-1: 1-protonated
0
1200000
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 3-protonated
0
3500000
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 2-protonated
0
30000000
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 3-protonated
0
110000000
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 0-protonated
0
330000000
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 2-protonated
0
350000000
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 1-protonated
0
1600000000
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 0-protonated
0
1900000000
collagen I alpha-2 chain
-
pH not specified in the publication, 37C, MMP-1: 1-protonated
0
58
type III collagen
-
pH 7.5, 25C, wild-type substrate
0
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, 37C
0.000143
2-[benzyl([[(4-chlorophenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
pH 6.0, 37C
0.000135
2-[benzyl([[(4-fluorophenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
pH 6.0, 37C
0.00017
2-[benzyl([[(4-methylphenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
pH 6.0, 37C
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
-
-
0.000032
3-[3-Benzoyl-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000025
3-[Benzenesulfonyl-(4-nitro-benzyl)-amino]-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
0.5
ClCH2CO-(N-OH)Leu-Ala-Gly-NH2
-
25C, pH 7.4, Tris buffer
2.5
ClCH2CO-(N-OH)Phe-Ala-Ala-NH2
-
25C, pH 7.4, Tris buffer
0.0000128
CT 1746
-
exon 5 mutant enzyme
-
0.0000603
CT 1746
-
wild-type enzyme
-
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
0.000039
N-2-methylphenylsulfonylureido-N-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37C
0.000036
N-2-methylphenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37C
0.000038
N-2-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37C
0.000029
N-2-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37C
0.000015
N-2-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37C
0.000024
N-4-chlorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37C
0.000024
N-4-chlorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37C
0.00019
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine
-
pH 6.0, 37C
0.00002
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37C
0.00023
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
pH 6.0, 37C
0.000014
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37C
0.000025
N-4-fluorophenylsulfonylureido-N-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37C
0.000021
N-4-fluorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37C
0.0002
N-4-fluorophenylsulfonylureido-N-[(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
pH 6.0, 37C
0.000021
N-4-fluorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37C
0.000013
N-4-fluorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37C
0.000017
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37C
0.00018
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
pH 6.0, 37C
0.000011
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37C
0.000032
N-4-methylphenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37C
0.00003
N-4-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37C
0.000018
N-4-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37C
0.000024
N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37C
0.000015
N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37C
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
-
-
0.000087
N-Hydroxy-3-[methanesulfonyl-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000025
N-phenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37C
0.000015
N-phenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37C
0.000013
N-phenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37C
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
0.0000108
Ro31-9790
-
wild-type enzyme
0.0001893
Ro31-9790
-
exon 5 mutant enzyme
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
-
-
-
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
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
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00001
batimastat
-
-
0.000005
marimastat
-
-
0.000003
trocade
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
-
quantitative MMP-1 expression analysis by RT-PCR in presence or absence of enzyme inhibitors
additional information
-
basal activity in different subjects, overview
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
-
skin and fibroblasts
6
-
assay at
6.5 - 7
-
-
6.5 - 7.5
-
-
7 - 7.4
-
uterus
7 - 8
-
skin
7.4
-
assay at
7.5 - 8.5
-
-
7.5
-
assay at
7.6
-
assay at
7.6
-
rheumatoid synovium
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
-
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; 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; degradation of synthetic substrate is pH-independent; 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
6.5 - 9.5
-
pH 6.5: about 65% of maximal activity, pH 9.5: about 60% of maximal activity
7 - 9.8
-
about 70% of maximal activity at pH 7.0 and at pH 9.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
assay at
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
in the center of granulomas
Manually annotated by BRENDA team
-
MMP-1 is upregulated in the infarcted tissue compared to healthy control areas
Manually annotated by BRENDA team
-
MMP-1 is upregulated by TGF-beta, EGF and IL-1beta
Manually annotated by BRENDA team
-
cell line JJ, increased MMP1 expression in chondrosarcoma, mechanism, overview
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
purified MMP-1 from synovial fibroblasts
Manually annotated by BRENDA team
-
acceleration of matrix metalloproteinase-1 production by oxidized low-sensity lipoprotein and 4-hydroxynonenal
Manually annotated by BRENDA team
-
of interleukin-1-treated dermal fibroblasts
Manually annotated by BRENDA team
-
of rheumatoid synovial cells stimulated with rabbit macrophage-conditioned medium
Manually annotated by BRENDA team
-
MMP-1 is expressed by migrating enterocytes bordering intestinal ulcers. In the fetal gut model, MMP-1 expression by migrating enterocytes is detected
Manually annotated by BRENDA team
-
primary epithelial ovarian tumor cell
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
primary cultured corneal and tenon's fibroblast
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
dermal, quantitative MMP-1 expression analysis by RT-PCR
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
NHDFs and NB1RGBs
Manually annotated by BRENDA team
-
primary lung fibroblast cell lines
Manually annotated by BRENDA team
-
dermal, primary
Manually annotated by BRENDA team
-
gingival, gingival fibroblasts produce MMP-1 in response to inflammatory cytokines, such as TNF and interleukin-1
Manually annotated by BRENDA team
-
synovial fibroblast
Manually annotated by BRENDA team
-
expression of MMP-1 is markedly increased by both onion extract and quercetin in vitro in human skin fibroblasts
Manually annotated by BRENDA team
-
expression of MMP-1 is markedly increased by both onion extract and quercetin in vivo in hairless mice
Manually annotated by BRENDA team
-
connective tissue
Manually annotated by BRENDA team
-
immortalized human keratinocyte cells
Manually annotated by BRENDA team
-
MMP-10 and MMP-1 are up-regulated in HaCaT II-4 cells
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
after hyperglycaemic treatment, expression of matrix metalloproteinase-1 and alpha2beta1 integrin is significantly downregulated
Manually annotated by BRENDA team
-
epidermal, primary, from foreskin
Manually annotated by BRENDA team
-
glycine-extended gastrin renders colon cancer cells more invasive by increasing MMP-I expression via the putative glycine-extended gastrin receptor
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
primary, monocyte-derived
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
high MMP-1 level
Manually annotated by BRENDA team
-
VMM5 cells, VMM12cells and VMM39. Constitutive overexpression of collagenase 1 is mediated by the ERK pathway in invasive melanoma cells
Manually annotated by BRENDA team
-
of invasive melanomas
Manually annotated by BRENDA team
-
Muller glia cell line
Manually annotated by BRENDA team
-
saphenous vein smooth muscle
Manually annotated by BRENDA team
-
expression profile of MMPs/TIMP-1 after myocardial infarction, angiotensin II receptor blockade improves MMPs/TIMP-1 balance, overview
Manually annotated by BRENDA team
-
UM1 and UM2 are oral tongue squamous cell carcinoma cell lines
Manually annotated by BRENDA team
-
ovarian clear cell carcinoma cell
Manually annotated by BRENDA team
-
collagen-induced arthritis hind paw sections as a model of human rheumatoid arthritis
Manually annotated by BRENDA team
Mus musculus DBA/1J
-
collagen-induced arthritis hind paw sections as a model of human rheumatoid arthritis
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
no differences in MMP-1 in the plasma of hypertensive versus normotensive subjects
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
MMP-1 is progressively decreased from prostate intraepithelial neoplasia to prostate carcinoma
Manually annotated by BRENDA team
-
enzyme expression is significantly stronger in the epithelium than in the stroma
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
from the lateral thoracic area of a 230 day fetal calf
Manually annotated by BRENDA team
-
all-trans retinoic acid suppresses matrix metalloproteinase activity in diabetic skin
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
a human chondrosarcoma cell line
Manually annotated by BRENDA team
-
fibroblast-like, from rheumatoid arthritis patients
Manually annotated by BRENDA team
Frog
-
backskin
Manually annotated by BRENDA team
-
from Achilles tendon, immunohistochemic analysis of MMP-1, overview
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
mononuclear phagocytes
Manually annotated by BRENDA team
-
leg ulcer tissue from patients with chronic venous insufficiency
Manually annotated by BRENDA team
-
MMP-1 is upregulated by EGF
Manually annotated by BRENDA team
additional information
-
MMP-1 expression analysis in gingival tissue, overview
Manually annotated by BRENDA team
additional information
-
MMP-1 is downregulated 4fold during trophoblast differentiation, reduced MMP-1 expression in pre-eclampsia and fetal growth restriction
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
additional information
-
selective cell-dependent MMP secretion
Manually annotated by BRENDA team
additional information
Mus musculus Sv129
-
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
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is secreted
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
-
MMP-1 is secreted
-
Manually annotated by BRENDA team
-
MMP-1 is secreted by skin fibroblasts
-
Manually annotated by BRENDA team
Mus musculus DBA/1J
-
the enzyme is secreted
-
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38000
-
gel filtration
95826
53000
-
calculated
665844
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 51929, the minor glycosylated enzyme form has a MW of 57000 Da, calculation from nucleotide sequence
?
-
x * 50000, exon 5 mutant species, SDS-PAGE, x * 58000, N-glycosylated exon 5 mutant species, SDS-PAGE
additional information
-
MMP-1A comprises a signal peptide and a propeptide, a catalytic domain and a hemopexin-like domain
additional information
Mus musculus Sv129
-
MMP-1A comprises a signal peptide and a propeptide, a catalytic domain and a hemopexin-like domain
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
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procollagenase
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
proteolytic modification
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procollagenase is activated by trypsin
proteolytic modification
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procollagenase activated by treatment with trypsin
proteolytic modification
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MMP-1 is activated from a pro-MMP-1 form
proteolytic modification
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pro-MMP1 is activated by plasmin to active MMP-1
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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small angle X-ray scattering
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
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complete and irreversible loss of activity
95827
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 60
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10 min, irreversible inactivation, little loss of activity below 50C
95827
90
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10 min, inactivation
95828
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type and exon 5 mutant enzyme
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recombinant His-tagged isolated MMP-1A catalytic domain by nickel affinity chromatography from Escherichia coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain BL21(DE3)
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expression analysis
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expression analysis of MMP1 in cancerous and healthy oral tissues, overview
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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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quantitative MMP-1 expression analysis
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quantitative MMP-1 expression analysis in primary dermal fibroblasts
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quantitative MMP-1 expression analysis in skin fibroblasts
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quantitative MMP-1 expression analysis, overview
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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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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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recombinant expression of His-tagged isolated MMP-1 catalytic domain as soluble cytoplasmic protein in Escherichia coli
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MMP-1 expression anaylsis, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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 suppression of MMP-1 gene expression
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dexamethasone, and less potent also interleukin-1Ra and TNF, decrease levels of pro-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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fucoidan treatment significantly inhibits the expression of MMP-1
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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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inhibition of MMP-1 expression by extracts of Kaempferia pandurata, overview
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inhibtitory effects of potent antioxidant astaxanthin on the MMP-1 induction by UV-A irradiation, overview
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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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Rac1 inhibitor NSC23766 suppresses MMP1 in dermal fibroblasts, and half-lives of type I collagen protein are increased
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SB203580 and PD98059 suppress MMP-1 secretion
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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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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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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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induction of MMP-1 by UV-A irradiation treatment of cultured human dermal fibroblasts
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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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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 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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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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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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expression of MMP-1 is markedly increased by both onion extract and quercetin in vitro in human skin fibroblasts
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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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expression of MMP-1 is markedly increased by both onion extract and quercetin in vivo in hairless mice
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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
Mus musculus DBA/1J
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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA243-340
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about 10% increase in turnover number and 9% increase in Km-value compared to wild-type enzyme with fTHP-3 as substrate
DELTA243-450
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the KM-value for the alpa1(I)772-786 triple-helical peptide is 3.3fold higher than that of the wild-type enzyme, the turnover number for this substrate is 2.5fold higher
R183Q/W184W/T185T/N186K/N187D/F188T/R189T/E190G/Y191T
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mutation reduces collagenolytic activity about 10fold
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
E219A
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inactive mutant
additional information
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construction of a chimeric enzyme, the exon 5 chimera, consisting primarily of MMP-1, with the region coded for by exon 5 replaced with the equivalent region of MMP-3, a noncollagenolytic MMP. Unlike MMP-3, the exon 5 chimera is capable of cleaving type I collagen, but the activity is only 2.2% of the trypsin-activated MMP-1. The kinetics for exon 5 chimera cleavage of two synthetic substrates display an MMP-3 phenotype, however, cleavage of gelatin is slightly impaired as compared to the parent enzymes. The KI-values for the exon 5 chimera complexed with synthetic inhibitors and N-terminal TIMP-2 show a more MMP-3-like behaviour. The exon 5 mutant shows a 2.9fold in the ratio of turnover number to Km-value with (7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-(3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2
additional information
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introduction of various lengths of MMP-1 segments into MMP-3, i.e. stromelysin 1, starting from the C-terminal end. MMP-3/MMP-1 chimeras and variants are overexpressed in Escherichia coli, folded from inclusion bodies and isolated as zymogens. The nine residues 183RWTNNFREY191 located between the fifth beta-strand and the second alpha-helix in the catalytic domain of MMP-1 are critical for the expression of collagenolytic activity
additional information
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MMP-1 enzyme inhibition and downregulation by short hairpin RNA, shRNA, reducing collagenase activity and angiogenesis of melanoma cells, but has no effect on primary tumor growth, xenograft modeling
additional information
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acid sphingomyelinase-deficient human fibroblasts fail to phosphorylate extracellular signal-regulated kinase, ERK, or upregulate MMP-1 mRNA and protein expression upon stimulation with interleukin-1 beta, overview. Transfection of acid sphingomyelinase restores MMP-1 production, while inhibition of acid sphingomyelinase with imipramine completely abrogates MMP-1 induction
additional information
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development of a piezoelectric immunosensor for matrix metalloproteinase-1 detection based on multilayered ultra-thin films composed by precursor layers of cationic poly(dimethyldiallylammonium) chloride and anionic poly(styrenesulfonate) with bound monolayer of antibodies, Layer by Layer self assembly technique, evaluation, overview
additional information
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disruption of the proximal AP-1-binding site in the promoter of MMP-1 severely impair MMP-1 transcription in response to bortezomib
additional information
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identification of a common functional polymorphism in the matrix metalloproteinase-1 gene promoter, 1G or 2G at nucleotide -1607, in individuals with epidermolysis bullosa pruriginosa compared with non-itchy dominant dystrophic epidermolysis bullosa, recessive dystrophic epidermolysis bullosa and healthy controls, overview. Genetic variants of a common functional polymorphism in the matrix metalloproteinase-1 gene promoter do not account for the itchy skin phenotype, overview
additional information
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overexpression of both ADAMTS1 and MMP-1 together increases osteolytic bone metastases, while overexpression of ADAMTS or MMP-1 alone has no effect
additional information
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transfection of oral tongue squamous cell carcinoma cells with microRNA candidates, including hsa-miR-222, reduces the expression of MMP1 and SOD2 in the cells, direct targeting of hsa-miR-222 to specific sequences located in the 3'-untranslated regions of both MMP1 and SOD2, overview
Y191T
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mutation reduces collagenolytic and gelatinolytic activity about 5fold
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
Mus musculus Sv129
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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
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
optimal folding occurs when the denatured protein is diluted at 4C 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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
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MMP-1 is an inflammation and senescent cell marker
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
diagnostics
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MMP-1 is an inflammation and senescent cell marker
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
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high level expression of MMP-14 and MMP-2 are observed in ovarian clear cell carcinoma relative to other histotypes
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
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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
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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
P03956
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
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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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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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MMP-1 suppressor Costaria costata fucoidan is a potential therapeutic agent for the prevention and treatment of photoaging of the skin
pharmacology
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MMP-1 is a potential target in therapy of melanoma
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
Mus musculus Sv129
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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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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