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Information on EC 3.4.24.17 - stromelysin 1 and Organism(s) Mus musculus and UniProt Accession P28862
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3.4.24.17 stromelysin 1Specify your search results
Word Map
- 3.4.24.17
- metalloproteinases
- mmp-1
- cartilage
- arthritis
- joint
- osteoarthritis
-
rheumatoid
- synovial
- chondrocytes
- necrosis
- timps
-
articular
- gelatinase
- tnf
- interleukin-1
- knee
-
zymography
- degeneration
- aggrecan
- proteoglycans
-
c-reactive
-
interstitial
- gelatin
- plasminogen
- proteinases
- cox-2
- synoviocytes
- il-1beta
-
fibroblast-like
-
cruciate
-
intervertebral
- ligament
- matrilysin
- pulposus
-
matrix-degrading
- adamts-4
- synovitis
- thrombospondin
-
intra-articular
-
subchondral
-
emmprin
-
chondroprotective
-
photoaging
- collagenases
- diagnostics
- medicine
- aggrecanase
-
prommp-9
-
neoepitope
-
gelatinolytic
- mt1-mmp
-
collagenolytic
- drug development
- analysis
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
mmp-3, stromelysin, matrix metalloproteinase-3, stromelysin-1, matrix metalloproteinase 3, transin, stromelysin 1, proteoglycanase, matrixin, matrix metalloprotease-3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Collagen-activating protein
-
-
-
-
Collagenase activating protein
-
-
-
-
Matrix metalloproteinase 3
MMP-3
Neutral proteoglycanase
-
-
-
-
Procollagenase activator
-
-
-
-
Proteoglycanase
-
-
-
-
PTR1 protein
-
-
-
-
Stromelysin
-
-
-
-
Transin
-
-
-
-
Matrix metalloproteinase 3
-
-
-
-
MMP-3
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
79955-99-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
enzyme attacks the basal lamina and tight junction proteins, opening the blood-brain barrier and thereby facilitating neutrophil influx
-
-
?
additional information
?
-
-
enzyme is expressed as a protective response and plays an important role in host defense during squamous cell carcinoma tumorigenesis
-
-
?
additional information
?
-
-
genetic ablation of MMP-3 does not significantly affect tumor growth and metastasis in the MMTV-PyMT model
-
-
?
additional information
?
-
-
MMPs belong to a family of over 20 neutral endopeptidases that are collectively able to cleave all extracellular matrix components as well as many non-extracellular matrix proteins. The stromelysins, MMP-3, MMP-10 and MMP-11, have a domain arrangement similar to that of collagenases, but they do not cleave interstitial collagens
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
enzyme attacks the basal lamina and tight junction proteins, opening the blood-brain barrier and thereby facilitating neutrophil influx
-
-
?
additional information
?
-
-
enzyme is expressed as a protective response and plays an important role in host defense during squamous cell carcinoma tumorigenesis
-
-
?
additional information
?
-
-
genetic ablation of MMP-3 does not significantly affect tumor growth and metastasis in the MMTV-PyMT model
-
-
?
additional information
?
-
-
MMPs belong to a family of over 20 neutral endopeptidases that are collectively able to cleave all extracellular matrix components as well as many non-extracellular matrix proteins. The stromelysins, MMP-3, MMP-10 and MMP-11, have a domain arrangement similar to that of collagenases, but they do not cleave interstitial collagens
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2(R)-[2-(4'-fluoro-4-biphenylyl)ethyl]-4-(S9-n-butyl-1,5-pentanedioic acid 1)-(alpha(S)-tert-butylglycine methylamide) amide
-
L-758,354
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(3'-trifluoromethyl-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4'-fluoro-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4'-trifluoromethyl-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-naphthalen-1-yl-phenyl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-naphthalen-2-yl-phenyl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-phenethyl-phenyl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-phenoxy-cyclohexa-1,5-dienyl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-propyl-phenyl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-styryl-phenyl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-thiophen-3-yl-phenyl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-phenyl-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-[4-(1H-indol-2-yl)-phenyl]-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-[4-(tetrahydro-furan-2-yl)-phenyl]-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-phenylcarbamoyl-propylcarbamoyl)-6-(4'-fluoro-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(2',6'-dimethyl-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(2'-fluoro-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(2'-sulfamoyl-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(3'-fluoro-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-formyl-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methanesulfinyl-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methanesulfonyl-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methoxy-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methylsulfanyl-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-[1,1',4',1'']terphenyl-4-yl-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-[4'-(1H-imidazol-2-yl)-biphenyl-4-yl]-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-[4'-(1H-tetrazol-5-yl)-biphenyl-4-yl]-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-[4'-[(N-methyl-aminooxy)-methyl]-biphenyl-4-yl]-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-{4'-[(N-methyl-aminooxy)-methyl]-biphenyl-4-yl}-hexanoic acid
-
-
2-Butyl-4-[2,2-dimethyl-1-(pyridin-4-ylcarbamoyl)-propylcarbamoyl]-6-(4'-fluoro-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[2,2-dimethyl-1-(pyridin-4-ylcarbamoyl)-propylcarbamoyl]-6-(4-propyl-phenyl)-hexanoic acid
-
-
2-Butyl-6-(2',4'-dichloro-biphenyl-4-yl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
-
2-Butyl-6-(3',5'-dichloro-biphenyl-4-yl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
-
2-Butyl-6-(3'-chloro-4'-fluoro-biphenyl-4-yl)-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
-
2-Butyl-6-(4'-chloro-biphenyl-4-yl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
-
2-Butyl-6-(4'-cyano-biphenyl-4-yl)-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
-
2-Butyl-6-(4-cycloheptyl-phenyl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
-
2-Butyl-6-[4'-(N,N-dimethyl-aminooxymethyl)-biphenyl-4-yl]-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
-
4'-[5-Carboxy-3-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-nonyl]-biphenyl-4-carboxylic acid
-
-
4'-[5-Carboxy-3-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-nonyl]-biphenyl-4-carboxylic acid methyl ester
-
-
4'-{5-Carboxy-3-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-nonyl}-biphenyl-4-carboxylic acid
-
-
4'-{5-Carboxy-3-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-nonyl}-biphenyl-4-carboxylic acid methyl ester
-
-
6-(3'-Amino-biphenyl-4-yl)-2-butyl-4-(2,2-dimethyl-1-phenylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
-
6-(4'-Aminooxymethyl-biphenyl-4-yl)-2-butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
-
6-(4'-Bromo-biphenyl-4-yl)-2-butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
-
6-(4-Benzyl-phenyl)-2-butyl-4-(2,2-dimethyl-1-phenylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
-
6-(4-Benzyloxy-phenyl)-2-butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
-
6-Biphenyl-4-yl-2-butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
-
curcumin
-
curcumin dose dependently suppresses MMP-3 and-9 activity during eradication of Helicobacter pylori from infected mice
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00013
L-asparaginyl-L-asparaginylglycyl-L-histidine
pH and temperature not specified in the publication
0.0011
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(3'-trifluoromethyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.00001
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4'-fluoro-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000037
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4'-trifluoromethyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.002
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-naphthalen-1-yl-phenyl)-hexanoic acid
-
pH 6.5, 25°C
0.00012
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-naphthalen-2-yl-phenyl)-hexanoic acid
-
pH 6.5, 25°C
0.00049
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-phenethyl-phenyl)-hexanoic acid
-
pH 6.5, 25°C
0.0002
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-phenoxy-cyclohexa-1,5-dienyl)-hexanoic acid
-
pH 6.5, 25°C
0.00014
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-propyl-phenyl)-hexanoic acid
-
pH 6.5, 25°C
0.00065
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-styryl-phenyl)-hexanoic acid
-
pH 6.5, 25°C
0.000015
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-thiophen-3-yl-phenyl)-hexanoic acid
-
pH 6.5, 25°C
0.0038
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-phenyl-hexanoic acid
-
pH 6.5, 25°C
0.000012
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-[4-(1H-indol-2-yl)-phenyl]-hexanoic acid
-
pH 6.5, 25°C
0.0014
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-[4-(tetrahydro-furan-2-yl)-phenyl]-hexanoic acid
-
pH 6.5, 25°C
0.000004
2-Butyl-4-(2,2-dimethyl-1-phenylcarbamoyl-propylcarbamoyl)-6-(4'-fluoro-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.0012
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(2',6'-dimethyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000011
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(2'-fluoro-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.0094
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(2'-sulfamoyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000021
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(3'-fluoro-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000015
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-formyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000052
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methanesulfinyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000021
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methanesulfonyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000013
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methoxy-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000005
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methylsulfanyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000039
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-[1,1',4',1'']terphenyl-4-yl-hexanoic acid
-
pH 6.5, 25°C
0.000025
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-[4'-(1H-imidazol-2-yl)-biphenyl-4-yl]-hexanoic acid
-
pH 6.5, 25°C
0.00035
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-[4'-(1H-tetrazol-5-yl)-biphenyl-4-yl]-hexanoic acid
-
pH 6.5, 25°C
0.000049
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-[4'-[(N-methyl-aminooxy)-methyl]-biphenyl-4-yl]-hexanoic acid
-
pH 6.5, 25°C
0.000002
2-Butyl-4-[2,2-dimethyl-1-(pyridin-4-ylcarbamoyl)-propylcarbamoyl]-6-(4'-fluoro-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000011
2-Butyl-4-[2,2-dimethyl-1-(pyridin-4-ylcarbamoyl)-propylcarbamoyl]-6-(4-propyl-phenyl)-hexanoic acid
-
pH 6.5, 25°C
0.000012
2-Butyl-6-(2',4'-dichloro-biphenyl-4-yl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25°C
0.0015
2-Butyl-6-(3',5'-dichloro-biphenyl-4-yl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25°C
0.000019
2-Butyl-6-(3'-chloro-4'-fluoro-biphenyl-4-yl)-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
pH 6.5, 25°C
0.000013
2-Butyl-6-(4'-chloro-biphenyl-4-yl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25°C
0.000009
2-Butyl-6-(4'-cyano-biphenyl-4-yl)-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
pH 6.5, 25°C
0.000095
2-Butyl-6-(4-cycloheptyl-phenyl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25°C
0.00004
2-Butyl-6-[4'-(N,N-dimethyl-aminooxymethyl)-biphenyl-4-yl]-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
pH 6.5, 25°C
0.00069
4'-[5-Carboxy-3-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-nonyl]-biphenyl-4-carboxylic acid
-
pH 6.5, 25°C
0.000031
4'-[5-Carboxy-3-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-nonyl]-biphenyl-4-carboxylic acid methyl ester
-
pH 6.5, 25°C
0.000027
6-(3'-Amino-biphenyl-4-yl)-2-butyl-4-(2,2-dimethyl-1-phenylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25°C
0.000024
6-(4'-Aminooxymethyl-biphenyl-4-yl)-2-butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
pH 6.5, 25°C
0.000011
6-(4'-Bromo-biphenyl-4-yl)-2-butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
pH 6.5, 25°C
0.0014
6-(4-Benzyl-phenyl)-2-butyl-4-(2,2-dimethyl-1-phenylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25°C
0.000074
6-(4-Benzyloxy-phenyl)-2-butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25°C
0.0015
6-Biphenyl-4-yl-2-butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
age-dependent increase in the central nervous system expression of MMP-3 in Twitcher mice suffering globoid cell leukodystrophy
unspecific staining in tissue sections of both animal strains with commercial anti-MMP-3 antibody JM3523 and positive but enzyme unspecific staining with the anti-MMP-3 antibody MAB 548 in both MMP-3 wild-type and MMP-3-deficient mouse skin wounds, antibody cross-reactivity due to the extreme similarity between MMP-3 and MMP-10 (EC 3.4.24.22) proteins
-
subcutaneous and gonadal adipose tissue. Significantly reduced MMP-3 expression in MMP-10-deficient adipose tissues
-
enzyme expression in transiently induced during specific intercellular contact with endothelial cells. Enzyme expression is tightly regulated upon lymphoma cell/stromal cell interaction
-
collagen-induced arthritis hind paw sections as a model of human rheumatoid arthritis
additional information
-
MMP-3 is strongly expressed in tumor and arthritis specimens, expression patterns of MMP-3 in a variety of healthy, cancerous and arthritic murine tissues, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
psychosine-induced globoid cell formation from microglia is prevented by either genetic ablation or chemical inhibition of enzyme MMP-3. Elevated expression of MMP-3 in globoid cell leukodystrophy or Krabbe disease, a fatal demyelinating disease, may promote microglial responses to psychosine that may represent an important pathophysiological process in this disease and its treatment
physiological function
matrix metalloproteinase (MMP)-3 mediates a morphological transformation of microglia into a multinucleated globoid cell type
malfunction
physiological function
-
MMP-3 participates in intimal hyperplasia in a mouse carotid artery ligation model and contributes to vessel remodeling
additional information
malfunction
-
knockout of MMP-3 attenuates vascular smooth muscle cell migration through reduced MMP-9 activation
additional information
bone marrow transplantation does not dampen elevated MMP-3 levels in globoid cell leukodystrophy-model Twitcher Mice
additional information
-
bone marrow transplantation does not dampen elevated MMP-3 levels in globoid cell leukodystrophy-model Twitcher Mice
additional information
unspecific staining in tissue sections of both animal strains with commercial anti-MMP-3 antibody JM3523 and positive but enzyme unspecific staining with the anti-MMP-3 antibody MAB 548 in both MMP-3 wild-type and MMP-3-deficient mouse skin wounds, antibody cross-reactivity due to the extreme similarity between MMP-3 and MMP-10 (EC 3.4.24.22) proteins
additional information
-
unspecific staining in tissue sections of both animal strains with commercial anti-MMP-3 antibody JM3523 and positive but enzyme unspecific staining with the anti-MMP-3 antibody MAB 548 in both MMP-3 wild-type and MMP-3-deficient mouse skin wounds, antibody cross-reactivity due to the extreme similarity between MMP-3 and MMP-10 (EC 3.4.24.22) proteins
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MMP3_MOUSE
477
0
53845
Swiss-Prot
Secretory Pathway (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
MMP-3 comprises a signal peptide and a propeptide, a catalytic domain and a hemopexin-like domain
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
MMP-3 deficient mice are crossed back to a homozygous BL10 background for 10 generations as described above. Male MMP-3 knock-out and BL10 wild-type mice are used for the experimental setting
additional information
-
MMP-3 deficient mice are crossed back to a homozygous BL10 background for 10 generations as described above. Male MMP-3 knock-out and BL10 wild-type mice are used for the experimental setting
additional information
-
enzyme overexpression im lymphoma transfectants significantly improves their ability to migrate through the matrix. Animals injected with lymphoma cells expressing enzyme constitutively develop thymic lymphoma more rapidly than those injected with control cells. Local expression of enzyme promotes lymphoma progression
additional information
-
Less disruption of blood-brain barrier after intracerebral lipopolysaccharide injection in enzyme knockout animals than in wild-type. Mutant animals show lower level of matrix metalloproteinase MMP-9 but similar levels of activation as wild-type
additional information
-
generation of specific recombinant human monoclonal antibody SP3, which is specific to the murine MMP-3 catalytic domain
additional information
-
MMP-3-/- mice kept on high fat diet show adipocyte hypertrophy in adipose tissues
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged isolated MMP-3 catalytic domain by nickel affinity chromatography from Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ectopical overexpression of C-terminally Strep-tagged mouse MMP-3 in HepG2 cells
recombinant expression of His-tagged isolated MMP-3 catalytic domain as soluble cytoplasmic protein in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
exposure of primary glial cultures to psychosine induces the expression and the production of matrix metalloproteinase-3 that mediates a morphological transformation of microglia into a multinucleated globoid cell type. But although psychosine treatment in primary purified microglial cultures moderately induces MMP-3 expression, treatment of peripheral blood or purified macrophages with equivalent concentrations of psychosine does not induce MMP-3 expression
lipopolysaccharide does not induce mmp-3 mRNA expression in peripheral blood samples
Curcumin dose dependently suppresses MMP-3 and -9 expression in Helicobacter pylori infected mouse gastric tissues
-
production of MMP-3 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
-
stromelysin-1 is slightly downregulated in obese adipose tissue compared to non-obese adipose tissue. Expression of MMP-3 mRNA in subcutaneous and gonadal adipose tissue is affected and 3.0-3.7fold reduced by MMP-10 deficiency, but vessel size is not affected
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
unspecific staining in tissue sections of both animal strains with commercial anti-MMP-3 antibody JM3523 and positive but enzyme unspecific staining with the anti-MMP-3 antibody MAB 548 in both MMP-3 wild-type and MMP-3-deficient mouse skin wounds
analysis
-
generation of specific recombinant human monoclonal antibody SP3, which may serve as building block for the development of antibody-based therapy strategies in mouse models of pathology
medicine
medicine
-
enzyme overexpression im lymphoma transfectants significantly improves their ability to migrate through the matrix. Animals injected with lymphoma cells expressing enzyme constitutively develop thymic lymphoma more rapidly than those injected with control cells. Local expression of enzyme promotes lymphoma progression
medicine
-
wild-type and enzyme null mutant animals, chemical carcinogenesis by 1-methyl-3-nitro-1-nitroso-guanidine or by 7,12-dimethylbenz[a]anthracene and 12-O-tetradecanoylphorbol-13-acetate. No difference in tumor onset or incidence between wild-type and enzyme null mutant animal, but tumors originating on mutant mice have enhanced initial tumor growth coupled with with an elevated proliferative index and reduced vasculature density
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Esser, C.K.; Bugianesi, R.L.; Caldwell, C.G.; Chapman, K.T.; Durette, P.L.; Girotra, N.N.; Kopka, I.E.; Lanza, T.J.; Levorse, D.A.; MacCoss, M.; Owens, K.A.; Ponpipom, M.M.; Simeone, J.P.; Harrison, R.K.; Niedzwiecki, L.; Becker, J.W.; Marcy, A.I.; Axel, M.G.; Christen, A.J.; McDonnell, J.; Moore, V.L.; Olszewski, J.M.; Saphos, C.; Visco, D.M.; Hagmann, W.K.; et al.
Inhibition of stromelysin-1 (MMP-3) by P1'-biphenylylethyl carboxyalkyl dipeptides
J. Med. Chem.
40
1026-1040
1997
Mus musculus, Rattus norvegicus, Mus musculus C57Bl6/J
Van Themsche, C.; Potworowski, E.F.; St-Pierre, Y.
Stromelysin-1 (MMP-3) is inducible in T lymphoma cells and accelerates the growth of lymphoid tumors in vivo
Biochem. Biophys. Res. Commun.
315
884-891
2004
Mus musculus
McCawley, L.J.; Crawford, H.C.; King, L.E.; Mudgett, J.; Matrisian, L.M.
A protective role for matrix metalloproteinase-3 in squamous cell carcinoma
Cancer Res.
64
6965-6972
2004
Mus musculus
Gurney, K.J.; Estrada, E.Y.; Rosenberg, G.A.
Blood-brain barrier disruption by stromelysin-1 facilitates neutrophil infiltration in neuroinflammation
Neurobiol. Dis.
23
87-96
2006
Mus musculus
Jin, X.; Yagi, M.; Akiyama, N.; Hirosaki, T.; Higashi, S.; Lin, C.Y.; Dickson, R.B.; Kitamura, H.; Miyazaki, K.
Matriptase activates stromelysin (MMP-3) and promotes tumor growth and angiogenesis
Cancer Sci.
97
1327-1334
2006
Mus musculus
Handley, S.A.; Miller, V.L.
General and specific host responses to bacterial infection in Peyers patches: a role for stromelysin-1 (matrix metalloproteinase-3) during Salmonella enterica infection
Mol. Microbiol.
64
94-110
2007
Mus musculus
Juncker-Jensen, A.; Romer, J.; Pennington, C.J.; Lund, L.R.; Almholt, K.
Spontaneous metastasis in matrix metalloproteinase 3-deficient mice
Mol. Carcinog.
48
618-625
2009
Mus musculus
Lijnen, H.R.; Van Hoef, B.; Rodriguez, J.A.; Paramo, J.A.
Stromelysin-2 (MMP-10) deficiency does not affect adipose tissue formation in a mouse model of nutritionally induced obesity
Biochem. Biophys. Res. Commun.
389
378-381
2009
Mus musculus
Pfaffen, S.; Hemmerle, T.; Weber, M.; Neri, D.
Isolation and characterization of human monoclonal antibodies specific to MMP-1A, MMP-2 and MMP-3
Exp. Cell Res.
316
836-847
2010
Mus musculus, Mus musculus Sv129
Mun, S.H.; Kim, H.S.; Kim, J.W.; Ko, N.Y.; Kim, D.K.; Lee, B.Y.; Kim, B.; Won, H.S.; Shin, H.S.; Han, J.W.; Lee, H.Y.; Kim, Y.M.; Choi, W.S.
Oral administration of curcumin suppresses production of matrix metalloproteinase (MMP)-1 and MMP-3 to ameliorate collagen-induced arthritis: inhibition of the PKCdelta/JNK/c-Jun pathway
J. Pharmacol. Sci.
111
13-21
2009
Homo sapiens, Mus musculus, Mus musculus DBA/1J
Johnson, J.L.; Dwivedi, A.; Somerville, M.; George, S.J.; Newby, A.C.
Matrix metalloproteinase (MMP)-3 activates MMP-9 mediated vascular smooth muscle cell migration and neointima formation in mice
Arterioscler. Thromb. Vasc. Biol.
31
e35-e44
2011
Mus musculus
Kundu, P.; De, R.; Pal, I.; Mukhopadhyay, A.; Saha, D.; Swarnakar, S.
Curcumin alleviates matrix metalloproteinase-3 and -9 activities during eradication of Helicobacter pylori infection in cultured cells and mice
PLoS ONE
6
e16306
2011
Homo sapiens, Mus musculus
Ijichi, K.; Brown, G.D.; Moore, C.S.; Lee, J.P.; Winokur, P.N.; Pagarigan, R.; Snyder, E.Y.; Bongarzone, E.R.; Crocker, S.J.
MMP-3 mediates psychosine-induced globoid cell formation: implications for leukodystrophy pathology
Glia
61
765-777
2013
Mus musculus (P28862), Mus musculus, Mus musculus C57BL/6 (P28862)
Mirastschijski, U.; Dinesh, N.; Baskaran, S.; Wedekind, D.; Gavrilovic, J.; Murray, M.Y.; Bevan, D.; Kelm, S.
Novel specific human and mouse stromelysin-1 (MMP-3) and stromelysin-2 (MMP-10) antibodies for biochemical and immunohistochemical analyses
Wound Repair Regen.
27
309-323
2019
Mus musculus (P28862), Mus musculus, Mus musculus BL10 (P28862)
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