Information on EC 3.4.24.17 - stromelysin 1

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

EC NUMBER
COMMENTARY
3.4.24.17
-
RECOMMENDED NAME
GeneOntology No.
stromelysin 1
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
preferential cleavage where P1', P2' and P3' are hydrophobic residues
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Collagen-activating protein
-
-
-
-
Collagenase activating protein
-
-
-
-
Matrix metalloproteinase 3
-
-
-
-
Matrix metalloproteinase 3
-
-
Matrix metalloproteinase 3
-
-
Matrix metalloproteinase 3
Mus musculus Sv129
-
-
-
matrix metalloproteinase-3
-
-
matrix metalloproteinase-3
Mus musculus DBA/1J
-
-
-
matrix metalloproteinase-3
-
-
matrixin
-
-
MMP-3
-
-
-
-
MMP-3
Mus musculus C57B/6J, Mus musculus DBA/1J, Mus musculus Sv129
-
-
-
Neutral proteoglycanase
-
-
-
-
Procollagenase activator
-
-
-
-
Proteoglycanase
-
-
-
-
PTR1 protein
-
-
-
-
Stromelysin
-
-
-
-
stromelysin-1
-
catalytic domain (residues 83-247) are used in this study
stromelysin-1
-
-
stromelysin-1
Mus musculus C57B/6J
-
-
-
stromelysin-1
-
-
stromelysin-1
-
-
Transin
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
79955-99-0
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
catalytic domain lacking both propeptide and C-terminal fragment; expression in Escherichia coli
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
expression in Escherichia coli; prostromelysin (treatment with (aminophenyl)mercuric acetate results in activation)
-
-
Manually annotated by BRENDA team
human
SwissProt
Manually annotated by BRENDA team
Koreans including Helicobacter pylori-infected subjects and Helicobacter pylori-negative controls
-
-
Manually annotated by BRENDA team
patients with active untreated adult onset Stills disease
-
-
Manually annotated by BRENDA team
patients with cutaneous malignant melanoma
-
-
Manually annotated by BRENDA team
prostromelysin expressed in a mouse fibroblast cell line C127 (self activation by incubation at 55C to a 45000 MW and a 28000 MW form)
-
-
Manually annotated by BRENDA team
truncated protein lacking C-terminus
-
-
Manually annotated by BRENDA team
women with or without endometriosis
-
-
Manually annotated by BRENDA team
cohort of 63 PyMT transgenic mice, either deficient for MMP-3 or wild-type controls
-
-
Manually annotated by BRENDA team
DBA/1J mice
-
-
Manually annotated by BRENDA team
male C57BL/6J mice
-
-
Manually annotated by BRENDA team
mouse, C57B/6J
-
-
Manually annotated by BRENDA team
Sv129 mice
-
-
Manually annotated by BRENDA team
wild-type and enzyme-null mutant animal
-
-
Manually annotated by BRENDA team
Mus musculus C57B/6J
mouse, C57B/6J
-
-
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
expression in hBRIe 380i cells. Both peptide YY and neuropeptide Y increase expression of enzyme to a level sufficient to induce cell migration by activating the Rho GTPase Cdc42. Peptide YY and neuropeptide Y modulate synchronously enzyme, CD63 and Cdc42
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
MMP-3 is involved in breast cancer cell invasiveness
malfunction
-
MMP-3 is involved in glioma cell invasion, overview
malfunction
-
MMP-3 is strongly expressed in tumor and arthritis specimens
malfunction
-
reduced MMP-3 expression in invasive trophoblasts of patients with severe preeclampsia
malfunction
-
knockout of MMP-3 attenuates vascular smooth muscle cell migration through reduced MMP-9 activation
malfunction
Mus musculus Sv129
-
MMP-3 is strongly expressed in tumor and arthritis specimens
-
metabolism
-
NF-kappaB and AP-1 are important transcription factors for MMP-3 gene expression. Glycitein, a bacterial metabolite of the isoflavone glycitin, inhibits glioma cell invasion through downregulation of MMP-3 and MMP-9 gene expression, overview
physiological function
-
MMP-3 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
-
inflammatory tissue destruction is central to pathology in cerebral tuberculosis with microglial-derived matrix metalloproteinases playing a key role in driving such damage
physiological function
-
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 MMPTIMP balance results in progressive destruction of gingival and periodontal extracellular matrix
physiological function
-
in addition to the decidua, MMP-3 of trophoblasts may contribute to the regulation of the IGF system by degrading IGFBP-1
physiological function
-
MMP-3 participates in intimal hyperplasia in a mouse carotid artery ligation model and contributes to vessel remodeling
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-Tyr-Ala-norvaline-Trp-Met-Lys(2,4-dinitrophenyl)-NH2 + H2O
?
show the reaction diagram
-
hydrolyzed 60 times more rapidly by metalloproteinase-3 than metalloproteinase-1, little discrimination between metalloproteinase-3 and metalloproteinase-2
-
-
-
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2 + H2O
?
show the reaction diagram
-
a fluorogenic substrate selectively hydrolyzed by stromelysin 1
-
-
-
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2 + H2O
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu + norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2
show the reaction diagram
-
-
-
-
(7-methoxycoumarin-4-yl)acetyl-P-L-G-L-(L)-2,3-diaminopropionylamide-A-R + H2O
?
show the reaction diagram
-
-
-
-
?
(7-Methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
(7-Methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly + Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2
show the reaction diagram
-
-
-
-
(7-Methoxycoumarin-4-yl)acetyl-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Lys-(2,4-dinitrophenyl)-Gly + H2O
?
show the reaction diagram
-
hydrolyzed equally well by metalloproteinase-3 and metalloproteinase-2, metalloproteinase-1 shows 25% of the activity compared to metalloproteinase-3
-
-
-
2,4-Dinitrophenyl-Arg-Pro-Lys-Pro-Leu-Ala-norvaline-Trp-NH2 + H2O
2,4-Dinitrophenyl-Arg-Pro-Lys-Pro-Leu-Ala + norvaline-Trp-NH2
show the reaction diagram
-
-
-
-
2,4-Dinitrophenyl-Pro-Leu-Gly-Ile-Ala-Gly-Arg-NH2 + H2O
?
show the reaction diagram
-
-
-
-
-
2,4-Dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH2 + H2O
2,4-Dinitrophenyl-Pro-Leu-Gly + Leu-Trp-Ala-D-Arg-NH2
show the reaction diagram
-
-
-
-
2,4-Dinitrophenyl-Pro-Tyr-Ala-Tyr-Trp-Met-Arg-NH2 + H2O
2,4-Dinitrophenyl-Pro-Tyr-Ala + Tyr-Trp-Met-Arg-NH2
show the reaction diagram
-
-
-
-
2,4-Dinitrophenyl-Pro-Tyr-Ala-Tyr-Trp-Met-Arg-NH2 + H2O
2,4-Dinitrophenyl-Pro-Tyr-Ala + Tyr-Trp-Met-Arg-NH2
show the reaction diagram
-
-
-
-
6-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]hexanoy-L-Arg-L-Pro-L-Lys-L-Pro-L-Leu-L-Ala-L-Nva-L-Trp-L-Lys(7-dimethylaminocoumarin-4-yl)-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
Acetyl-Pro-Leu-Gly-thioester-Leu-Leu-Gly ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
-
acetyl-Pro-Leu-Gly-[2-mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5 + H2O
?
show the reaction diagram
-
-
-
-
?
Aggrecan core protein + H2O
?
show the reaction diagram
-
-
-
-
-
alpha-Proteinase inhibitor + H2O
2,4-Dinitrophenyl-Pro-Leu-Gly + Ile-Ala-Gly-Arg-NH2
show the reaction diagram
-
-
-
-
alpha-Proteinase inhibitor + H2O
2,4-Dinitrophenyl-Pro-Leu-Gly + Ile-Ala-Gly-Arg-NH2
show the reaction diagram
-
alpha1-proteinase inhibitor, cleavage within the reactive site loop
-
-
alpha1-Antichymotrypsin + H2O
?
show the reaction diagram
-
cleaves at the P1'-P2' bond
-
-
-
alpha1-antitrypsin + H2O
?
show the reaction diagram
-
-
-
-
?
Antithrombin III + H2O
?
show the reaction diagram
-
cleavage of the P1-P1' bond in the reactive center
-
-
-
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Nle-NH2 + H2O
?
show the reaction diagram
-
-
-
-
-
Azocoll + H2O
?
show the reaction diagram
-
-
-
-
-
beta-casein + H2O
?
show the reaction diagram
-
-
-
-
?
Carboxymethyltransferrin + H2O
?
show the reaction diagram
-
-
-
-
-
cartilage + H2O
?
show the reaction diagram
Mus musculus, Rattus norvegicus, Mus musculus C57B/6J
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
-
casein + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
-
casein + H2O
?
show the reaction diagram
-
casein zymography assay
-
-
?
casein + H2O
?
show the reaction diagram
-
casein zymography assay method
-
-
?
decorin + H2O
transforming growth factor-beta + ?
show the reaction diagram
-
-
-
?
DQ-collagen I + H2O
?
show the reaction diagram
-
-
-
-
?
DQ-collagen IV + H2O
?
show the reaction diagram
-
-
-
-
?
Elastin + H2O
?
show the reaction diagram
-
-
-
-
-
Elastin + H2O
?
show the reaction diagram
-
-
-
-
-
Elastin + H2O
?
show the reaction diagram
-
limited activity
-
-
-
elastin fELN-125 + H2O
?
show the reaction diagram
-
-
-
-
?
fibrin + H2O
fibrin fragments + ?
show the reaction diagram
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
Intact fibronectin subunit MW 22000 + a disulfide-bonded COOH-terminal MW 20000 polypeptide
show the reaction diagram
-
-
-
-
Fibronectin + H2O
Intact fibronectin subunit MW 22000 + a disulfide-bonded COOH-terminal MW 20000 polypeptide
show the reaction diagram
-
-
-
-
Fibronectin + H2O
Intact fibronectin subunit MW 22000 + a disulfide-bonded COOH-terminal MW 20000 polypeptide
show the reaction diagram
-
-
-
-
Fibronectin + H2O
Intact fibronectin subunit MW 22000 + a disulfide-bonded COOH-terminal MW 20000 polypeptide
show the reaction diagram
-
-
-
-
Fibronectin + H2O
Intact fibronectin subunit MW 22000 + a disulfide-bonded COOH-terminal MW 20000 polypeptide
show the reaction diagram
-
-
-
-
Fibronectin + H2O
Intact fibronectin subunit MW 22000 + a disulfide-bonded COOH-terminal MW 20000 polypeptide
show the reaction diagram
-
-
-
-
FS-6 + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
-
Gelatin + H2O
?
show the reaction diagram
-
limited activity
-
-
-
Gelatin + H2O
?
show the reaction diagram
-
type 1
-
-
-
Gelatin + H2O
?
show the reaction diagram
-
type 1
-
-
-
Immunoglobulin G2a + H2O
?
show the reaction diagram
-
-
-
-
-
Laminin + H2O
?
show the reaction diagram
-
-
-
-
-
Laminin + H2O
?
show the reaction diagram
-
-
-
-
-
Laminin + H2O
?
show the reaction diagram
-
limited activity
-
-
-
Laminin + H2O
?
show the reaction diagram
-
cleavage activity is barely detected as a much lower activity as reported
-
-
?
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys (Dnp) + H2O
?
show the reaction diagram
-
-
-
-
?
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 + H2O
?
show the reaction diagram
-
fluorogenic substrate
-
-
?
NFF2 + H2O
?
show the reaction diagram
quenched fluorescence substrate
-
-
?
osteopontin + H2O
?
show the reaction diagram
-
-
-
-
?
Procollagen + H2O
?
show the reaction diagram
-
removal of the NH2-terminal propeptides
-
-
-
Procollagen + H2O
?
show the reaction diagram
-
removal of the NH2-terminal propeptides
-
-
-
triple helical peptide alpha1(V) + H2O
?
show the reaction diagram
-
collagen V fibrils
-
-
?
Collagen type III + H2O
?
show the reaction diagram
-
-
-
-
-
Collagen type IV + H2O
additional information
-
-
-
-
-
Collagen type IV + H2O
additional information
-
-
-
-
-
Collagen type IV + H2O
additional information
-
-
-
-
-
Collagen type IV + H2O
additional information
-
-
-
-
-
Collagen type IV + H2O
additional information
-
-
-
4 major fragments of MW 165000, 145000, 125000 and 110000
-
Collagen type IV + H2O
additional information
-
-
no degradation of type I collagen, limited activity
-
-
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
show the reaction diagram
Mus musculus, Mus musculus Sv129
-
fluorogenic substrate
-
-
?
additional information
?
-
-
degradation of glomerular basement membrane
-
-
-
additional information
?
-
-
activates procollagenase
-
-
-
additional information
?
-
-
activates procollagenase
-
-
-
additional information
?
-
-
activates progelatinase B
-
-
-
additional information
?
-
-
enzyme is secreted from the cells as an inactive zymogen
-
-
-
additional information
?
-
-
degrades a number of extracellular matrix components
-
-
-
additional information
?
-
-
participates in activation of procollagenases and progelatinase B
-
-
-
additional information
?
-
-
cleavage sites in natural proteins
-
-
-
additional information
?
-
-
cleavage at multiple chondroitin sulfate-binding sites along the protein core
-
-
-
additional information
?
-
-
tyoe I collagen is no substrate
-
-
?
additional information
?
-
-
may play a role in the normal turnover of the connective tissue matrix as well as in the joint destruction of chronic synovitis
-
-
-
additional information
?
-
-
believed to play a role in pathological conditions such as arthritis and tumor invasion
-
-
-
additional information
?
-
-
glomerular basement membrane degradation by glomeruli may be attributable to stromelysin and suggest an important role for these proteinases in glomerular pathophysiology
-
-
-
additional information
?
-
-
degrading all of the major macromolecules of the extracellular matrix
-
-
?
additional information
?
-
-
required for the degradation of extracellular matrix components during normal embryo development, morphogenesis and tissue remodelling
-
-
?
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
?
-
-
stromelysin (MMP3), through its action on collagen and other matrix metalloproteinases, influences arterial wall remodeling
-
-
-
additional information
?
-
-
matrix metalloproteinases are endopeptidases capable of cleaving various components of extracellular matrix
-
-
-
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
-
-
-
Procollagen + H2O
?
show the reaction diagram
-
chicken type I
-
-
-
Proteoglycan + H2O
additional information
-
-
-
-
-
Proteoglycan + H2O
additional information
-
-
-
-
-
Proteoglycan + H2O
additional information
-
-
-
-
-
Proteoglycan + H2O
additional information
-
-
-
-
-
Proteoglycan + H2O
additional information
-
-
cartilage
degradation to 12.0 S fragments by the HMW form and 10.3 S fragments by the KMW enzyme
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
may play a role in the normal turnover of the connective tissue matrix as well as in the joint destruction of chronic synovitis
-
-
-
additional information
?
-
-
believed to play a role in pathological conditions such as arthritis and tumor invasion
-
-
-
additional information
?
-
-
glomerular basement membrane degradation by glomeruli may be attributable to stromelysin and suggest an important role for these proteinases in glomerular pathophysiology
-
-
-
additional information
?
-
-
degrading all of the major macromolecules of the extracellular matrix
-
-
?
additional information
?
-
-
required for the degradation of extracellular matrix components during normal embryo development, morphogenesis and tissue remodelling
-
-
?
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
?
-
-
stromelysin (MMP3), through its action on collagen and other matrix metalloproteinases, influences arterial wall remodeling
-
-
-
additional information
?
-
-
matrix metalloproteinases are endopeptidases capable of cleaving various components of extracellular matrix
-
-
-
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+
-
removal of Ca2+ from the enzyme solution results in a complete loss of activity that can be fully restored by addition of 1 mM Ca2+
Ca2+
-
Ca2+ is required to maintain the active conformation of the enzyme, full activity is detected at 1 mM Ca2+, at pH 7.5 and is retained at even higher concentrations of Ca2+, at lower concentrations the enzyme is autolyzed; proenzyme contains 3 Ca2+
Ca2+
-
calcium-dependent
Ca2+
-
calcium-dependent endopeptidase
Ca2+
-
-
Ca2+
-
-
Co2+
-
addition of 0.5 mM Co2+ in the presence of Ca2+ restores activity of the apoenzyme, not by Co2+ alone
Zinc
-
Zn2+: addition of 0.5 mM Zn2+ in the presence of Ca2+ restores activity of the apoenzyme, not by Zn2+ alone
Zinc
-
proenzyme and mature active form contain nearly 2 mol of Zn/mol of protein, location at the active site, zinc-cysteine interaction is required for the preservation of latency
Zinc
-
zinc metalloprotein, proenzyme contains two Zn2+, the Zn2+ at the active site is bound to His-201, His-205, and His-211 and Cys-75 in the propeptide
Zn2+
-
Glu202.zinc.H2O complex, zinc-dependent
Zn2+
-
zinc-containing endopeptidase
Zn2+
-
zinc endopeptidase
Zn2+
-
catalytic zinc atom is coordinated by H201, H205, H211
Zn2+
-
a zinc-containing endopeptidase
Zn2+
-
dependent on
Mn2+
-
addition of 5 mM Mn2+ in the presence of Ca2+ restores activity of the apoenzyme, not by Mn2+ alone
additional information
-
metalloproteinase
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2S)-2-((R)-sec-butyl)-N-hydroxy-3-((4-methoxyphenyl)sulfonyl)cyclopropanecarboxamide
-
-
(1R,3S)-N-hydroxy-2-((4-methoxyphenyl)sulfonyl)-3-((pyridin-3-yloxy)methyl)cyclopropanecarboxamide
-
-
(1R,3S)-N-hydroxy-2-((4-methoxyphenyl)sulfonyl)-3-(5-phenylpentyl)cyclopropanecarboxamide
-
-
(2S)-3-(4-fluorophenyl)-N-methyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
-
(2S)-3-(benzyloxy)-N-methyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
-
(2S)-3-phenyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
-
(2S)-3-phenyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
computational modeling of enzyme-inhibitor complex
(2S)-N-methyl-3-(4-nitrophenyl)-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
-
(2S)-N-methyl-3-(pentafluorophenyl)-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
i.e. PNU-142372
(2S)-N-methyl-3-(pentafluorophenyl)-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
i.e. PNU-142372, computational modeling of enzyme-inhibitor complex
(2S)-N-methyl-3-phenyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
i.e. PNU-107859
(2S)-N-methyl-3-phenyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
i.e. PNU-107859, computational modeling of enzyme-inhibitor complex
(betaR)-beta-[[[(1S)-1-[[[(1S)-2-methoxy-1-phenylethyl]amino]carbonyl]-2,2-dimethylpropyl]amino]carbonyl]-2-methyl-[1,1'-biphenyl]-4-hexanoic acid
-
UK-370106-COOH, potent inhibitor
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1-([[4-(3,4-dimethylphenoxy)phenyl]sulfonyl]methyl)-N-hydroxy-4-(prop-2-yn-1-yl)cyclohexanecarboxamide
-
-
1-acetyl-N-hydroxy-4-[[4-(phenylsulfanyl)phenyl]sulfonyl]piperidine-4-carboxamide
-
-
1-cyclopropyl-N-hydroxy-4-[(4-phenoxyphenyl)sulfonyl]piperidine-4-carboxamide
-
-
1-cyclopropyl-N-hydroxy-4-[[4-(phenylsulfanyl)phenyl]sulfonyl]piperidine-4-carboxamide
-
-
1-[(1S)-1-(4-fluorobenzyl)-2-oxo-2-(4-pyridin-2-ylpiperazin-1-yl)ethyl]-3-(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)urea
-
-
1-[(1S)-2-oxo-1-(pentafluorobenzyl)-2-(4-pyridin-2-ylpiperazin-1-yl)ethyl]-3-(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)urea
-
-
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(R)-[2-(4'-fluoro-4-biphenylyl)ethyl]-4-(S9-n-butyl-1,5-pentanedioic acid 1)-(alpha(S)-tert-butylglycine methylamide) amide
-
compound 26, L-758,354
2-([4-[3'-(2-aminoethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-N-hydroxy-2-methylpropanamide
-
-
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
-
-
2-[(2-biphenyl-4-ylethyl)(methyl)sulfamoyl]-N-hydroxyacetamide
-
-
2-[(3-biphenyl-4-ylazetidin-1-yl)sulfonyl]-N-hydroxyacetamide
-
-
2-[(3-biphenyl-4-ylpropyl)(methyl)sulfamoyl]-N-hydroxyacetamide
-
-
2-[(4-biphenyl-4-yl-3,6-dihydropyridin-1(2H)-yl)sulfonyl]-N-hydroxyacetamide
-
-
2-[(4-biphenyl-4-ylpiperidin-1-yl)sulfonyl]-N-hydroxyacetamide
-
-
2-[(4-[3'-[2-(dimethylamino)ethoxy]-2-methylbiphenyl-4-yl]piperidin-1-yl)sulfonyl]-N-hydroxy-2-methylpropanamide
-
-
2-[(biphenyl-4-ylmethyl)(methyl)sulfamoyl]-N-hydroxyacetamide
-
-
2-[(biphenyl-4-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide
-
-
2-[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide
-
-
2-[[2-(hydroxyamino)-2-oxoethyl][(4-phenoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide
-
-
2-[[3-(biphenyl-4-yloxy)azetidin-1-yl]sulfonyl]-N-hydroxyacetamide
-
-
2-[[4-(2,3'-dimethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
2-[[4-(2-chlorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
2-[[4-(2-ethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
2-[[4-(2-fluorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)piperidin-1-yl]sulfonyl]-N-hydroxy-2-methylpropanamide
-
-
2-[[4-(3'-ethyl-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
3-(4'-cyanobiphenyl-4-yloxy)-N-hydroxypropionamide
-
-
3-(hydroxycarbamoyl)-1-[(4-phenoxybenzoyl)amino]pentyl 2,2-dimethylpropanoate
-
-
3-ethyl-N-hydroxy-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethylprolinamide
-
-
3-[(4'-cyanobiphenyl-4-yl)oxy]-N-hydroxypropanamide
-
-
3-[(benzyloxy)methyl]-N-hydroxy-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethylprolinamide
-
-
3-[(benzylsulfanyl)methyl]-N-hydroxy-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethylprolinamide
-
-
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
-
-
4-(1-benzofuran-2-yl)-N-[(2S)-1-hydroxy-5-(hydroxyamino)-5-oxopentan-2-yl]benzamide
-
-
4-(1-benzofuran-2-yl)-N-[(2S)-2-hydroxy-4-(hydroxyamino)-4-oxobutyl]benzamide
-
-
4-(1-benzofuran-2-yl)-N-[(2S)-4-(hydroxyamino)-2-(methoxymethoxy)-4-oxobutyl]benzamide
-
-
4-(1-benzofuran-2-yl)-N-[(2S)-5-(hydroxyamino)-1-(methoxymethoxy)-5-oxopentan-2-yl]benzamide
-
-
4-(1-benzofuran-2-yl)-N-[(3R)-3-[(benzyloxy)methyl]-4-(hydroxyamino)-4-oxobutyl]benzamide
-
-
4-(1-benzofuran-2-yl)-N-[(3S)-3-hydroxy-4-(hydroxyamino)-4-oxobutyl]benzamide
-
-
4-(1-benzofuran-2-yl)-N-[3-(hydroxycarbamoyl)-6-phenylhexyl]benzamide
-
-
4-(1-benzofuran-2-yl)-N-[3-benzyl-4-(hydroxyamino)-4-oxobutyl]benzamide
-
-
4-(1-benzofuran-2-yl)-N-[4-(hydroxyamino)-4-oxobutyl]benzamide
-
-
4-(hydroxyamino)-3-methyl-4-oxo-1-[(4-phenoxybenzoyl)amino]butyl 2,2-dimethylpropanoate
-
-
4-([[4-(4-chlorophenoxy)phenyl]sulfonyl]methyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-([[4-(biphenyl-4-yloxy)phenyl]sulfonyl]methyl)-N-hydroxy-1-(2-phenylethyl)piperidine-4-carboxamide
-
-
4-([[4-(biphenyl-4-yloxy)phenyl]sulfonyl]methyl)-N-hydroxypiperidine-4-carboxamide
-
-
4-Aminobenzoyl-Gly-Pro-D-Leu-D-Ala-NHOH
-
-
4-[(E)-2-(4-chlorophenyl)ethenyl]-N-[4-(hydroxyamino)-4-oxobutyl]benzamide
-
-
4-[[4-(4-chlorophenoxy)phenyl]sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
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
-
-
alendronate
-
-
Alpha-macroglobulin
-
-
-
alpha-[[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]-carbonyl]amino]-3-hydroxy-N-methyl-(S)-propanamide
-
-
alpha-[[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]-carbonyl]amino]-3-hydroxy-N-methyl-(S)-propanamide
-
computational modeling of enzyme-inhibitor complex
alpha-[[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]carbonyl]amino]-N,N-dimethyl-(S)-benzenepropanamide
-
-
alpha-[[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]carbonyl]amino]-N,N-dimethyl-(S)-benzenepropanamide
-
computational modeling of enzyme-inhibitor complex
amide substituted piperazine-based MMP inhibitor
-
-
-
batimastat
-
-
benzyl [3-[(biphenyl-4-ylsulfonyl)(propan-2-yloxy)amino]-4-(hydroxyamino)-4-oxobutyl]carbamate
-
-
bisphosphonate
-
-
-
butanolic extract of propolis sample
-
-
-
carboxylic acid diphenylpiperidine inhibitor
-
-
-
CGS 27023
-
chicoric acid
-
-
clodronate
-
-
curcumin
-
curcumin dose dependently suppresses MMP-3 and-9 activity during eradication of Helicobacter pylori from infected mice
cysteine
-
-
daidzein
-
-
dexamethasone
-
inhibits active MMP-3, significantly decreases the ratio of active MMP-3 to total MMP-3 activity
dichloro[[(methylsulfinyl-kappaS)methyl]phosphonate-kappaO'']platinum
-
-
EDTA
-
-
EGTA
-
-
galardin
-
Glycomed GM-6001, clinically advanced MMP inhibitor, effective in treatment of corneal ulcers
genistein
-
-
genistin
-
-
HONH-CO-CH2-CH(n-pentyl)-CO-Leu-Phe-NH2
-
-
Hydroxamate-containing peptide inhibitor
-
-
-
hydroxamic acid diphenylpiperidine inhibitor
-
-
-
hydroxamic acid inhibitor CGS 27023
-
-
hydroxamic acid substrate mimetic inhibitor
-
U24522
-
interleukin-1 receptor antagonist
-
inhibits active MMP-3
-
kaempferol
-
-
N-(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)-N'-(2-phenethyl)urea
-
-
N-(biphenyl-4-ylsulfonyl)-N-[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]glycine
-
-
N-(Carboxyalkyl)dipeptide
-
Ala[N]homophenylalanine-Leu-anilide
-
N-alkyl-and heterocycle-substitited piperazine-based MMP inhibitor
-
-
-
N-hydroxy-1-(2-methoxyethyl)-4-[(4-phenoxyphenyl)sulfonyl]piperidine-4-carboxamide
-
-
N-hydroxy-1-(2-methoxyethyl)-4-[[4-(phenylsulfanyl)phenyl]sulfonyl]piperidine-4-carboxamide
-
-
N-hydroxy-1-methyl-4-[[4-(phenylsulfanyl)phenyl]sulfonyl]piperidine-4-carboxamide
-
-
N-hydroxy-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethyl-3-[[(2-phenylethyl)sulfanyl]methyl]prolinamide
-
-
N-hydroxy-1-[(methylsulfonyl)oxy]-4-[[4-(phenylsulfanyl)phenyl]sulfonyl]piperidine-4-carboxamide
-
-
N-hydroxy-1-[[(4-phenoxyphenyl)sulfonyl]methyl]-4-(prop-2-yn-1-yl)cyclohexanecarboxamide
-
-
N-hydroxy-2-([4-[2-(trifluoromethyl)biphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
-
-
N-hydroxy-2-([4-[2-methyl-3'-(trifluoromethoxy)biphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
-
-
N-hydroxy-2-([4-[3'-(2-hydroxyethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-2-methylpropanamide
-
-
N-hydroxy-2-([4-[3'-(2-methoxyethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-2-methylpropanamide
-
-
N-hydroxy-2-([4-[3'-(methoxymethyl)-2-methylbiphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
-
-
N-hydroxy-2-methyl-2-[(4-[2-methyl-3'-[2-(methylamino)ethoxy]biphenyl-4-yl]piperidin-1-yl)sulfonyl]propanamide
-
-
N-hydroxy-2-[(4-[4-[6-(2-hydroxyethoxy)pyridin-2-yl]-3-methylphenyl]piperidin-1-yl)sulfonyl]-2-methylpropanamide
-
-
N-hydroxy-2-[N-(2-hydroxyethyl)biphenyl-4-sulfonamide] hydroxamic acid
-
-
N-hydroxy-2-[[4-(2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]acetamide
-
-
N-hydroxy-2-[[4-(3'-methoxy-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]acetamide
-
-
N-hydroxy-2-[[4-(4-phenoxyphenyl)piperidin-1-yl]sulfonyl]acetamide
-
-
N-hydroxy-3-(hydroxymethyl)-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethylprolinamide
-
-
N-hydroxy-3-[(1R)-1-hydroxy-2-(phenylsulfanyl)ethyl]-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethylprolinamide
-
-
N-hydroxy-3-[(1S)-1-hydroxy-2-(phenylsulfanyl)ethyl]-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethylprolinamide
-
-
N-hydroxy-3-[[(4-methoxybenzyl)sulfanyl]methyl]-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethylprolinamide
-
-
N-hydroxy-4-[(4-phenoxyphenyl)sulfonyl]-1-(prop-2-yn-1-yl)piperidine-4-carboxamide
-
-
N-hydroxy-4-[(4-phenoxyphenyl)sulfonyl]piperidine-4-carboxamide
-
-
N-hydroxy-4-[[(4-phenoxyphenyl)sulfonyl]methyl]-1-(2-phenylethyl)piperidine-4-carboxamide
-
-
N-hydroxy-4-[[4-(phenylsulfanyl)phenyl]sulfonyl]-1-(prop-2-en-1-yl)piperidine-4-carboxamide
-
-
N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]-N2-(2-methylpropyl)phenyl-D-methioninamide
-
-
N-isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid
-
-
N-methyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)acetamide
-
-
N-methyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)acetamide
-
computational modeling of enzyme-inhibitor complex
N-[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]-N-[(4-methoxyphenyl)sulfonyl]glycine
-
-
N-[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]-N-[(4-phenoxyphenyl)sulfonyl]glycine
-
-
N-[1-(ethoxymethoxy)-3-(hydroxycarbamoyl)pentyl]-4-phenoxybenzamide
-
-
N-[1-(ethoxymethoxy)-4-(hydroxyamino)-3-methyl-4-oxobutyl]-4-phenoxybenzamide
-
-
N-[1-hydroxy-4-(hydroxyamino)-3-methyl-4-oxobutyl]-4-phenoxybenzamide
-
-
N-[3-(hydroxycarbamoyl)-1-[(2-methoxyethoxy)methoxy]pentyl]-4-phenoxybenzamide
-
-
N-[4-(hydroxyamino)-1-[(2-methoxyethoxy)methoxy]-3-methyl-4-oxobutyl]-4-phenoxybenzamide
-
-
N-[4-(hydroxyamino)-3-methyl-4-oxobutyl]-4-phenoxybenzamide
-
-
N-[4-(hydroxyamino)-4-oxobutyl]-4-phenoxybenzamide
-
-
N-[4-(hydroxyamino)-4-oxobutyl]-4-[(E)-2-(4-hydroxyphenyl)ethenyl]benzamide
-
-
N-[4-(hydroxyamino)-4-oxobutyl]-4-[(E)-2-(4-methoxyphenyl)ethenyl]benzamide
-
-
N-[4-(hydroxycarbamoyl)-1-(methoxymethoxy)-5,5-dimethylhexan-2-yl]-4-phenoxybenzamide
-
-
N-[4-(hydroxycarbamoyl)-1-(methoxymethoxy)-7,7-dimethyl-6-oxooctan-2-yl]-4-phenoxybenzamide
-
-
N-[4-(hydroxycarbamoyl)-1-(methoxymethoxy)hept-6-en-2-yl]-4-phenoxybenzamide
-
-
N-[4-(hydroxycarbamoyl)-1-(methoxymethoxy)heptan-2-yl]-4-phenoxybenzamide
-
-
N-[4-(hydroxycarbamoyl)-1-(methoxymethoxy)hexan-2-yl]-4-phenoxybenzamide
-
-
N-[4-(hydroxycarbamoyl)-1-(methoxymethoxy)octan-2-yl]-4-phenoxybenzamide
-
-
N-[4-hydroxy-5-(hydroxyamino)-1-(methoxymethoxy)-5-oxopentan-2-yl]-4-phenoxybenzamide
-
-
N-[5-(hydroxyamino)-1-(methoxymethoxy)-4-(naphthalen-1-ylmethyl)-5-oxopentan-2-yl]-4-phenoxybenzamide
-
-
N-[5-(hydroxyamino)-1-(methoxymethoxy)-4-methyl-5-oxopentan-2-yl]-4-phenoxybenzamide
-
-
N-[5-(hydroxyamino)-1-(methoxymethoxy)-5-oxo-4-(1l4-thiopyran-1-yl)pentan-2-yl]-4-phenoxybenzamide
-
-
N-[5-(hydroxyamino)-1-(methoxymethoxy)-5-oxo-4-(pyridin-2-ylmethyl)pentan-2-yl]-4-phenoxybenzamide
-
-
N-[5-(hydroxyamino)-1-(methoxymethoxy)-5-oxo-4-(pyridin-3-ylmethyl)pentan-2-yl]-4-phenoxybenzamide
-
-
N-[5-(hydroxyamino)-1-(methoxymethoxy)-5-oxo-4-(pyridin-4-ylmethyl)pentan-2-yl]-4-phenoxybenzamide
-
-
N-[5-(hydroxyamino)-1-(methoxymethoxy)-5-oxopentan-2-yl]-4-phenoxybenzamide
-
-
N-[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]carbonyl]-L-phenylalanine methyl ester
-
-
N2-(biphenyl-4-ylsulfonyl)-N-hydroxy-N2-(propan-2-yloxy)glycinamide
-
-
N2-(biphenyl-4-ylsulfonyl)-N-hydroxy-N2-(propan-2-yloxy)valinamide
-
-
Ovostatin
-
-
-
pamidronate
-
-
PD166793
-
-
PD180557
-
-
Peptides based on the N-terminal domain of tissue inhibitor of metalloproteinase-1
-
-
-
Phthaloyl-N-(CH2)4-P(O2-)-Ile-(2-naphthyl)-Ala-NH-CH3
-
-
quercetin
-
-
SM-25453
-
-
Specific metalloproteinase inhibitor
-
isolated from human amniotic fluid
-
Specific metalloproteinase inhibitor
-
bovine-nasal cartilage extract; isolated from human amniotic fluid; rabbit bone culture medium
-
sulfonamide-and carbamide substituted piperazine-based MMP inhibitor
-
-
-
TIMP
-
-
-
TIMP-1
-
-
-
TIMP-1
-
upregulated with age
-
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
-
physiolocic inhibitor of matrix metalloproteinases
-
TIMP-2
-
-
-
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 metalloproteinases
-
TIMP-1 and TIMP-2
-
TNF
-
inhibits active MMP-3
-
U24522
-
synthetic inhibitor known to inhibit proteoglycan-degrading metalloproteinases
UK-370106
-
-
UK-370106-COCHO
-
glyoxal inhibitor, created by conversion of the carboxylate group of UK-370106-COOH to a glyoxal group. At pH 5.5-6.5 the glyoxal inhibitor is a potent inhibitor of stromelysin-1
urea substituted piperazine-based MMP inhibitor
-
-
-
zoledronate
-
-
[dimethylpropanedioato(2-)-kappa2O1,O3][[(methylsulfinyl-kappaS)methyl]phosphonate-kappaO''']platinum
-
-
L-696,418
-
-
additional information
-
not: inhibitors for serine, cysteine or aspartic proteinases
-
additional information
-
diisopropylphosphofluoridate; pepstatin; phenylmethanesulfonyl fluoride; soybean trypsin inhibitor
-
additional information
-
not: inhibitors for serine, cysteine or aspartic proteinases; phosphoramidon
-
additional information
-
X-ray diffraction analysis of the three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme
-
additional information
-
the flavonols quercetin and kaempferol have higher anti-invasion potency and higher MMP-3 inhibitory activity than isoflavones genistein, genistin and daidzein, but neither flavonols nor isoflavones have any effect on MMP-3 secretion
-
additional information
-
ligand binding, inhibitory potencies, 3D-QSAR modelling, and crystal structures, overview. Usage of multitemplate alignment method for the development of a 3D QSAR model
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
beta-hematin
-
induces differential autocatalysis of the propeptide
Hemin
-
induces differential autocatalysis of the propeptide
p-aminophenylmercuric acetate
-
i.e. APMA, initiates an MMP-3 autocatalytic mechanism by disturbing the interaction of zinc with a critical cysteine residue
plasmin
-
-
-
Trypsin
-
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.066
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Tyr-Ala-norvaline-Trp-Met-Lys(2,4-dinitrophenyl)-NH2
-
-
0.025
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2
-
-
0.05
(7-Methoxycoumarin-4-yl)acetyl-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Lys-(2,4-dinitrophenyl)-Gly
-
-
0.1
2,4-Dinitrophenyl-Pro-Tyr-Ala-Tyr-Trp-Met-Arg-NH2
-
-
0.27
acetyl-Pro-Leu-Gly-thioester-Leu-Leu-Gly-ethylester
-
-
0.395
acetyl-Pro-Leu-Gly-[2-mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5
-
pH 6.0, 25C, catalytic domain (residues 83-247)
-
0.9
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-norleucine-NH2
-
wild-type enzyme form
1.4
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-norleucine-NH2
-
truncated enzyme form
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.95
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Tyr-Ala-norvaline-Trp-Met-Lys(2,4-dinitrophenyl)-NH2
Homo sapiens
-
-
5.4
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2
Homo sapiens
-
-
0.53
(7-Methoxycoumarin-4-yl)acetyl-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Lys-(2,4-dinitrophenyl)-Gly
Homo sapiens
-
-
0.24
2,4-Dinitrophenyl-Pro-Tyr-Ala-Tyr-Trp-Met-Arg-NH2
Homo sapiens
-
-
2.12
Acetyl-Pro-Leu-Gly-thioester-Leu-Leu-Gly ethyl ester
Homo sapiens
-
-
0.9
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Nle-NH2
Homo sapiens
-
wild-type enzyme form
1.35
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Nle-NH2
Homo sapiens
-
truncated enzyme form
0.085
beta-casein
Homo sapiens
-
pH 7.5, 37C, truncated enzyme
-
0.088
beta-casein
Homo sapiens
-
pH 7.5, 37C, truncated enzyme
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.6
acetyl-Pro-Leu-Gly-[2-mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5
Escherichia coli
-
pH 6.0, 25C, catalytic domain (residues 83-247)
86846
14.04
DQ-collagen I
Homo sapiens
-
pH 7.5, 25C
168024
0.11
DQ-collagen IV
Homo sapiens
-
pH 7.5, 25C
161170
0.83
elastin fELN-125
Homo sapiens
-
pH 7.5, 25C
168023
20.63
FS-6
Homo sapiens
-
pH 7.5, 25C
168022
0.048
triple helical peptide alpha1(V)
Homo sapiens
-
pH 7.5, 25C, value below
168025
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0001
(2S)-3-(4-fluorophenyl)-N-methyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
pH 7.6, 25C
0.002
(2S)-3-(benzyloxy)-N-methyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
pH 7.6, 25C
0.0033
(2S)-3-phenyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
pH 7.6, 25C
0.00033
(2S)-N-methyl-3-(4-nitrophenyl)-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
pH 7.6, 25C
0.000018
(2S)-N-methyl-3-(pentafluorophenyl)-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
pH 7.6, 25C
0.00071
(2S)-N-methyl-3-phenyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
pH 7.6, 25C
0.00027
1-[(1S)-1-(4-fluorobenzyl)-2-oxo-2-(4-pyridin-2-ylpiperazin-1-yl)ethyl]-3-(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)urea
-
pH 7.6, 25C
0.000014
1-[(1S)-2-oxo-1-(pentafluorobenzyl)-2-(4-pyridin-2-ylpiperazin-1-yl)ethyl]-3-(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)urea
-
pH 7.6, 25C
0.0011
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(3'-trifluoromethyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25C
0.00001
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4'-fluoro-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25C
0.000037
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4'-trifluoromethyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25C
0.002
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-naphthalen-1-yl-phenyl)-hexanoic acid
-
pH 6.5, 25C
0.00012
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-naphthalen-2-yl-phenyl)-hexanoic acid
-
pH 6.5, 25C
0.00049
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-phenethyl-phenyl)-hexanoic acid
-
pH 6.5, 25C
0.0002
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-phenoxy-cyclohexa-1,5-dienyl)-hexanoic acid
-
pH 6.5, 25C
0.00014
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-propyl-phenyl)-hexanoic acid
-
pH 6.5, 25C
0.00065
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-styryl-phenyl)-hexanoic acid
-
pH 6.5, 25C
0.000015
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-thiophen-3-yl-phenyl)-hexanoic acid
-
pH 6.5, 25C
0.0038
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-phenyl-hexanoic acid
-
pH 6.5, 25C
0.000012
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-[4-(1H-indol-2-yl)-phenyl]-hexanoic acid
-
pH 6.5, 25C
0.0014
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-[4-(tetrahydro-furan-2-yl)-phenyl]-hexanoic acid
-
pH 6.5, 25C
0.000004
2-Butyl-4-(2,2-dimethyl-1-phenylcarbamoyl-propylcarbamoyl)-6-(4'-fluoro-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25C
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, 25C
0.000011
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(2'-fluoro-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25C
0.0094
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(2'-sulfamoyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25C
0.000021
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(3'-fluoro-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25C
0.000015
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-formyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25C
0.000052
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methanesulfinyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25C
0.000021
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methanesulfonyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25C
0.000013
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methoxy-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25C
0.000005
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methylsulfanyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25C
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, 25C
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, 25C
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, 25C
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, 25C
0.000002
2-Butyl-4-[2,2-dimethyl-1-(pyridin-4-ylcarbamoyl)-propylcarbamoyl]-6-(4'-fluoro-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25C
0.000011
2-Butyl-4-[2,2-dimethyl-1-(pyridin-4-ylcarbamoyl)-propylcarbamoyl]-6-(4-propyl-phenyl)-hexanoic acid
-
pH 6.5, 25C
0.000012
2-Butyl-6-(2',4'-dichloro-biphenyl-4-yl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25C
0.0015
2-Butyl-6-(3',5'-dichloro-biphenyl-4-yl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25C
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, 25C
0.000013
2-Butyl-6-(4'-chloro-biphenyl-4-yl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25C
0.000009
2-Butyl-6-(4'-cyano-biphenyl-4-yl)-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
pH 6.5, 25C
0.000095
2-Butyl-6-(4-cycloheptyl-phenyl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25C
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, 25C
0.00025
3-(4'-cyanobiphenyl-4-yloxy)-N-hydroxypropionamide
-
-
0.00069
4'-[5-Carboxy-3-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-nonyl]-biphenyl-4-carboxylic acid
-
pH 6.5, 25C
0.000031
4'-[5-Carboxy-3-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-nonyl]-biphenyl-4-carboxylic acid methyl ester
-
pH 6.5, 25C
0.000027
6-(3'-Amino-biphenyl-4-yl)-2-butyl-4-(2,2-dimethyl-1-phenylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25C
0.000024
6-(4'-Aminooxymethyl-biphenyl-4-yl)-2-butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
pH 6.5, 25C
0.000011
6-(4'-Bromo-biphenyl-4-yl)-2-butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
pH 6.5, 25C
0.0014
6-(4-Benzyl-phenyl)-2-butyl-4-(2,2-dimethyl-1-phenylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25C
0.000074
6-(4-Benzyloxy-phenyl)-2-butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25C
0.0015
6-Biphenyl-4-yl-2-butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25C
0.031
alpha-[[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]-carbonyl]amino]-3-hydroxy-N-methyl-(S)-propanamide
-
pH 7.6, 25C
0.0023
alpha-[[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]carbonyl]amino]-N,N-dimethyl-(S)-benzenepropanamide
-
pH 7.6, 25C
0.000013
hydroxamic acid inhibitor CGS 27023
-
pH 6.8, 37C
0.00031
L-696,418
-
pH 6.5, 25C
0.007
N-(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)-N'-(2-phenethyl)urea
-
pH 7.6, 25C
0.00018
N-hydroxy-2-[N-(2-hydroxyethyl)biphenyl-4-sulfonamide] hydroxamic acid
-
-
0.0013
N-isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid
-
-
0.166
N-methyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)acetamide
-
pH 7.6, 25C
0.00029
N-[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]carbonyl]-L-phenylalanine methyl ester
-
pH 7.6, 25C
0.001
UK-370106-COCHO
-
pH 5.5-6.5, 25C
0.0107
UK-370106-COCHO
-
pH 7.56, 37C
0.0188
UK-370106-COCHO
-
pH 7.56, 25C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000004
2-([4-[3'-(2-aminoethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-N-hydroxy-2-methylpropanamide
Homo sapiens
-
-
0.000164
2-[(2-biphenyl-4-ylethyl)(methyl)sulfamoyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.000161
2-[(3-biphenyl-4-ylazetidin-1-yl)sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.000174
2-[(3-biphenyl-4-ylpropyl)(methyl)sulfamoyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.000006
2-[(4-biphenyl-4-yl-3,6-dihydropyridin-1(2H)-yl)sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.000026
2-[(4-biphenyl-4-ylpiperidin-1-yl)sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.000001
2-[(4-[3'-[2-(dimethylamino)ethoxy]-2-methylbiphenyl-4-yl]piperidin-1-yl)sulfonyl]-N-hydroxy-2-methylpropanamide
Homo sapiens
-
-
0.000378
2-[(biphenyl-4-ylmethyl)(methyl)sulfamoyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.00043
2-[(biphenyl-4-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide
Homo sapiens
-
pH 7.5, 25C
0.00014
2-[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide
Homo sapiens
-
pH 7.5, 25C
0.0000061
2-[[2-(hydroxyamino)-2-oxoethyl][(4-phenoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide
Homo sapiens
-
pH 7.5, 25C
0.000084
2-[[3-(biphenyl-4-yloxy)azetidin-1-yl]sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.000004
2-[[4-(2,3'-dimethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.000055
2-[[4-(2-chlorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.000402
2-[[4-(2-ethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.000003
2-[[4-(2-fluorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.000004
2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.000002
2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)piperidin-1-yl]sulfonyl]-N-hydroxy-2-methylpropanamide
Homo sapiens
-
-
0.000031
2-[[4-(3'-ethyl-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.00063
chicoric acid
Homo sapiens
-
pH and temperature not specified in the publication
0.3
clodronate
Homo sapiens
-
-
0.0053
dichloro[[(methylsulfinyl-kappaS)methyl]phosphonate-kappaO'']platinum
Homo sapiens
-
-
0.000127
N-(biphenyl-4-ylsulfonyl)-N-[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]glycine
Homo sapiens
-
pH 7.5, 25C
0.00096
N-hydroxy-2-([4-[2-(trifluoromethyl)biphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
Homo sapiens
-
-
0.000051
N-hydroxy-2-([4-[2-methyl-3'-(trifluoromethoxy)biphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
Homo sapiens
-
-
0.000001
N-hydroxy-2-([4-[3'-(2-hydroxyethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-2-methylpropanamide
Homo sapiens
-
-
0.000003
N-hydroxy-2-([4-[3'-(2-methoxyethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-2-methylpropanamide
Homo sapiens
-
-
0.000003
N-hydroxy-2-([4-[3'-(methoxymethyl)-2-methylbiphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
Homo sapiens
-
-
0.0000003
N-hydroxy-2-methyl-2-[(4-[2-methyl-3'-[2-(methylamino)ethoxy]biphenyl-4-yl]piperidin-1-yl)sulfonyl]propanamide
Homo sapiens
-
-
0.000001
N-hydroxy-2-[(4-[4-[6-(2-hydroxyethoxy)pyridin-2-yl]-3-methylphenyl]piperidin-1-yl)sulfonyl]-2-methylpropanamide
Homo sapiens
-
-
0.000016
N-hydroxy-2-[[4-(2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]acetamide
Homo sapiens
-
-
0.000005
N-hydroxy-2-[[4-(3'-methoxy-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]acetamide
Homo sapiens
-
-
0.000205
N-hydroxy-2-[[4-(4-phenoxyphenyl)piperidin-1-yl]sulfonyl]acetamide
Homo sapiens
-
-
0.000163
N-hydroxy-3-(hydroxymethyl)-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethylprolinamide
Homo sapiens
-
pH 7.5, 25C
0.000182
N-[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]-N-[(4-methoxyphenyl)sulfonyl]glycine
Homo sapiens
-
pH 7.5, 25C
0.0000067
N-[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]-N-[(4-phenoxyphenyl)sulfonyl]glycine
Homo sapiens
-
pH 7.5, 25C
0.00002
N-[4-(hydroxycarbamoyl)-1-(methoxymethoxy)-7,7-dimethyl-6-oxooctan-2-yl]-4-phenoxybenzamide
Homo sapiens
-
pH 7.5, 25C
0.0000372
N-[5-(hydroxyamino)-1-(methoxymethoxy)-4-methyl-5-oxopentan-2-yl]-4-phenoxybenzamide
Homo sapiens
-
pH 7.5, 25C
0.0000012
N-[5-(hydroxyamino)-1-(methoxymethoxy)-5-oxo-4-(pyridin-2-ylmethyl)pentan-2-yl]-4-phenoxybenzamide
Homo sapiens
-
pH 7.5, 25C
0.00138
N-[5-(hydroxyamino)-1-(methoxymethoxy)-5-oxopentan-2-yl]-4-phenoxybenzamide
Homo sapiens
-
pH 7.5, 25C
0.000023
UK-370106
Homo sapiens
-
-
0.0044
[dimethylpropanedioato(2-)-kappa2O1,O3][[(methylsulfinyl-kappaS)methyl]phosphonate-kappaO''']platinum
Homo sapiens
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000498
-
-
18.6
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
assay methods
additional information
-
basal activity in different subjects, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.3 - 5.5
-
digestion of aggrecan core protein
5.5
-
optimum for proteoglycan monomer, digestion of fibronectin and gelatin is more extensive at pH 5.5 than at pH 7.5
6
-
acetyl-Pro-Leu-Gly-thioester-Leu-Leu-Gly-ethylester
6
-
assay at
6
-
assay at
6 - 8.6
-
glomerular basement membrane
6.2
-
azocoll
7.4
-
assay at
7.5
-
assay at
7.5 - 7.8
-
-
7.6
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7.5
-
pH 5.0: about 20% of activity maximum, pH 7.5: about 25% of activity maximum
5 - 9
-
active over this range against various substrates
6 - 8.5
-
about 50% of activity maximum at pH 6.0 and 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
assay at
25
-
assay at
37
-
assay at
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
subcutaneous and gonadal adipose tissue. Significantly reduced MMP-3 expression in MMP-10-deficient adipose tissues
Manually annotated by BRENDA team
-
in the center of granulomas
Manually annotated by BRENDA team
-
MMP-3 is upregulated in the infarcted tissue compared to healthy control areas
Manually annotated by BRENDA team
-
of rheumatoid synovial cells
Manually annotated by BRENDA team
-
synovial fibroblasts
Manually annotated by BRENDA team
-
synovial fibroblasts
Manually annotated by BRENDA team
-
gastric epithelial cell
Manually annotated by BRENDA team
-
cultured skin fibroblast. Induction of enzyme and matrix metalloproteinase MMP-1 expression by heat shock. Suppression of induction by the inhibition of extracellular signal-regulated kinase and c-Jun N-terminal kinase and by specific inhibition of interleukin IL-6 by monoclonal antibody
Manually annotated by BRENDA team
-
gingival, gingival fibroblasts produce MMP-3 in response to inflammatory cytokines, such as TNF and interleukin-1
Manually annotated by BRENDA team
-
clinical phenotypes with Helicobacter pylori infection are strongly related to inflammatory cytokines, MMP-3, and pepsinogen secretion
Manually annotated by BRENDA team
-
induced by acetic acid injection
Manually annotated by BRENDA team
-
connective tissue
Manually annotated by BRENDA team
-
elevated expression of hippocampal enzyme mRNA and protein after traumatic brain injury. Enzyme is primarily localized to cell bodies within the deafferented dendritic laminae. Traumatic brain injury alone elevates enzyme protein over the stratum lacunosum moleculare, inner molecular layer and hilus, while traumatic brain injury plus bilateral entorhinal cortical lesion increases enzyme protein within the deafferented stratum lacunosum moleculare and dentate molecular layer
Manually annotated by BRENDA team
-
enzyme expression in transiently induced during specific intercellular contact with endothelial cells. Enzyme expression is tightly regulated upon lymphoma cell/stromal cell interaction
Manually annotated by BRENDA team
-
a human invasive breast carcinoma cell line
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
-
distribution and activity of MMP-3 in placenta, overview
Manually annotated by BRENDA team
-
no differences in MMP-3 in the plasma of hypertensive versus normotensive subjects
Manually annotated by BRENDA team
-
quantitative detection of pro- and active forms of MMP-3 in blood from healthy subjects of both genders and different ages, overview. MMP-3 and TIMP-1 serum levels are age-dependently increased, the relationship between age and MMP-3 serum levels is stronger in men compared to women
Manually annotated by BRENDA team
-
serum MMP-3 is significantly elevated in ankylosing spondylitis patients with active disease
Manually annotated by BRENDA team
-
trophoblatsic cell line
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
-
pro- and active form of MMP-3 are predominantly expressed in purified first trimester villous trophoblasts, in invasive cytotrophoblasts of differentiating explant cultures and in trophoblastic SGHPL-4 cells. Reduced MMP-3 expression in invasive trophoblasts of patients with severe preeclampsia
Manually annotated by BRENDA team
-
astroglioma cells
Manually annotated by BRENDA team
additional information
-
the enzyme is not readily detected in normal cells in culture or tissue homogenates, but its synthesis is greatly enhanced in mesenchymal cells when they are treated with cytokines such as interleukin-1 and tumor necrosis factor alpha, growth factors, phorbol myristate, acetate and several other stimuli
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
additional information
-
MMP-3 expression analysis in gingival tissue, overview
Manually annotated by BRENDA team
additional information
-
selective cell-dependent MMP secretion
Manually annotated by BRENDA team
additional information
-
comparison of basal and interleukin-1beta-dependent MMP-3 expression in SGHPL-4 cells and decidual fibroblasts, overview
Manually annotated by BRENDA team
additional information
Mus musculus Sv129
-
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
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
MMP-3 is secreted
-
Manually annotated by BRENDA team
-
the enzyme is secreted, determination of MMP-3 in cell culture medium
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
-
active MMP-3 is secreted
-
Manually annotated by BRENDA team
Mus musculus DBA/1J
-
the enzyme is secreted
-
-
Manually annotated by BRENDA team
additional information
-
invasive trophoblast cell models secrete bioactive MMP-3
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24500
-
gel filtration
31004
57000
-
-
649839
additional information
-
human, latent precursor, MW 51000, gel filtration
31002
additional information
-
proenzyme form of 51000 MW is activated during isolation to several forms: 41000 MW form after treatment with trypsin or 4-aminophenylmercuric acetate, active forms of MW 21000-25000 and the activatable form of MW 35000
31003
additional information
-
prostromelysin expressed in a mouse fibroblast cell line C127 self activates by incubation at 55C to a 45000 MW and a 28000 MW form
31014
additional information
-
stromelysin 1 is synthesized as a preproenzyme of 477 amino acids and is secreted from cells as a proenzyme of 460 amino acids which consist of the propeptide (82 amino acids), the catalytic domain (165 amino acids), the proline-rich region (25 amino acids), and the C-terminal domain (188 amino acids)
31017
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 28000, human, form LMW, SDS-PAGE; x * 45000, human, form HMW, SDS-PAGE
?
-
x * 12500, rabbit, SDS-PAGE
?
-
x * 57000, pro-MMP-3, SDS-PAGE, x * 45000, mature MMP-3, SDS-PAGE
monomer
-
-
additional information
-
MMP-3 comprises a signal peptide and a propeptide, a catalytic domain and a hemopexin-like domain
additional information
Mus musculus Sv129
-
MMP-3 comprises a signal peptide and a propeptide, a catalytic domain and a hemopexin-like domain
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
proenzyme is proteolytically activated by plasmin. C18 unsaturated fatty acids are inhibitory, with elaidic acid totally abolishing the activation. Inhibitory effect result from binding of unsaturated fatty acids to kringle 5
proteolytic modification
-
pro-MMP-3 autoactivates to mature MMP-3, initiated by p-aminophenylmercuric acetate
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with inhibitor
-
in complex with inhibitor SM-25453, comparison with structure of EC 3.4.24.B4 with inhibitor
-
selenomethionine-substituted C-terminally truncated proMMP-3(DELTAC), sitting drop vapour-diffusion technique, crystals belong to tetragonal space group P4(3), cell axes a = b = 80.62 A, c = 157.62 A
-
catalytic domain of MMP-3 in complex with a P1-biphenyl inhibitor
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
-
more than 80% loss of activity after 15 h
31017
4.5
-
at pHs 4.5 and 10.0 irreversible denaturation is biphasic
717280
5
-
about 50% loss of activity after 15 h
31017
5
-
at pHs 5.0 and 9.0 there is exponential irreversible denaturation with half lives of 38 and 68 min, respectively
717280
5.5 - 9.5
-
stable in this range
31017
6 - 9
-
37C, stable
31012
6.8 - 8.4
-
stable for at least 16 h at pHs 6.0-8.4
717280
9
-
at pHs 5.0 and 9.0 there is exponential irreversible denaturation with half lives of 38 and 68 min, respectively
717280
10
-
about 50% loss of activity after 15 h
31017
10
-
at pHs 4.5 and 10.0 irreversible denaturation is biphasic
717280
10.5
-
more than 80% loss of activity after 15 h
31017
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
stable at pH 6-9
31012
37
-
48 h, stable, prostromelysin
31017
80
-
15 min: 35% loss activity of enzyme form HMW, 5% loss of sctivity of enzyme form LMW
31002
80
-
15 min, 35% loss of activity
31017
100
-
15 min, 65% loss of activity of enzyme form HMW, 25% loss of activity of enzyme form LMW
31002
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+ is required to maintain the active conformation, full activity is detected at 1 mM Ca2+, at pH 7.5 and is retained at even higher concentrations of Ca2+, at lower concentrations the enzyme is autolyzed
-
Ca2+ stabilizes
-
catalytic domain of MMP-12 exhibits higher activity, more rigidity of its backbone, and lower folding stability than its counterpart of theMMP-3 catalytic domain that has more internal motions throughout
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 0C or 4C, 50 mM Tris-HCl, pH 7.5, 0.4 M NaCl, 10 mM Ca2+, 0.05% Brij 35, 0.02% NaN3, less than 19% loss of activity after 10 weeks
-
-20C, 50 mM Tris-HCl, pH 7.5, 0.15 M NaCl, 10 mM CaCl2, 0.02% w/v NaN3, 0.05% w/v Brij 35, stable for at least 1 year, prostromelysin 1
-
4C, 50 mM Tris-HCl, pH 7.5, 0.15 M NaCl, 10 mM CaCl2, 0.02% w/v NaN3, 0.05% w/v Brij 35, stable for at least 4 months, prostromelysin 1
-
4C, 50 mM Tris-HCl, pH 7.6, 10 mM CaCl2, stable
-
4C, latent and active form, stable for 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified from Escherichia coli
-
2 active forms: HMW, LMW
-
C-terminally truncated protein; expression in Escherichia coli
-
catalytic domain lacking both propeptide and C-terminal fragment; expression in Escherichia coli
-
expression in Escherichia coli; prostromelysin (treatment with (aminophenyl)mercuric acetate results in activation)
-
prostromelysin expressed in a mouse fibroblast cell line C127 (self activation by incubation at 55C to a 45000 MW and a 28000 MW form)
-
recombinant enzyme
-
recombinant SCD
-
recombinant His-tagged isolated MMP-3 catalytic domain by nickel affinity chromatography from Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catalytic domain expressed in Escherichia coli
-
gene encoding ST1 expressed in lepidopteran Sf9 cells infected with recombinant baculovirus
-
NF-kappaB and AP-1 are important transcription factors for MMP-3 gene expression. Glycitein inhibits the promoter activitiy of MMP-3, overview
-
recombinant SCD expressed in Escherichia coli
-
selenomethionine-substituted C-terminally truncated proMMP-3(DELTAC) expressed in Escherichia coli B834(DE3)
-
recombinant expression of His-tagged isolated MMP-3 catalytic domain as soluble cytoplasmic protein in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
interleukin-1Ra, dexamethasone, and TNF significantly decrease levels of all forms of MMP-3
-
glycitein, i.e. 4',7-dihydroxy-6-methoxyisoflavone, a bacterial metabolite of the isoflavone glycitin, downregulates MMP-3 gene expression by inhibiting the promoter activity of MMP-3
-
dexamethasone suppression of MMP-3 gene expression
-
expression of MMP-3 in cartilages and synovial tissues is suppressed by the treatment of curcumin and indomethacin. Production of MMP-3 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
-
reduced MMP-3 expression in invasive trophoblasts of patients with severe preeclampsia
-
Curcumin dose dependently suppresses MMP-3 and -9 expression in Helicobacter pylori infected human gastric epithelial cells
-
MMP-3 expression is upregulated with age, overview
-
TNF-alpha and interleukin-1beta act synergistically to drive MMP-3 secretion. NF-kappaB and AP-1 c-Jun/FosB heterodimers regulate CoMTb-induced MMP-3 secretion. NF-kappaB p65 and AP-1 c-Jun subunits are upregulated in biopsy granulomas from patients with cerebral tuberculosis. CoMTb upregulates MMP-3 gene expression and secretion in microglia
-
MMP-3 is induced in gingival fibroblasts in response to inflammatory cytokines, such as TNF and interleukin-1
-
TNF-alpha and IL-1beta stimulate production of MMPs through the activation of mitogen-activated protein kinases, NF-kappaB and AP-1
-
MMP-3 is upregulated after stroke in brain in the infarcted tissue compared to healthy control areas, overview
-
MMP-3 is induced by interleukin-1beta, which, despite its effects on MMP-3 expression, fails to significantly alter invasion of SGHPL-4 cells through Matrigel-coated transwells
-
serum MMP-3 is significantly elevated in ankylosing spondylitis patients with active disease
-
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
-
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
-
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
Mus musculus DBA/1J
-
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
catalytic domain (residues 83-247) are used in this study
E219A
-
NMR studies used MMP-12 preserved by E219A substitution of the general base
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
-
MMP-3-/- mice kept on high fat diet show adipocyte hypertrophy in adipose tissues
additional information
-
generation of specific recombinant human monoclonal antibody SP3, which is specific to the murine MMP-3 catalytic domain
additional information
Mus musculus Sv129
-
generation of specific recombinant human monoclonal antibody SP3, which is specific to the murine MMP-3 catalytic domain
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
important target for inhibitor design and synthesis because of the widespread implications in arthritis, cancer, and cardiovascular disease
medicine
-
attractive target for pharmaceutical design, implicated in diseases such as arthritis and cancer
medicine
-
MMP inhibitor development is the target of considerable effort within the pharmaceutical industry, MMP activity can contribute to the pathologies of cancer invasion and metastasis, arthritis, autoimmune disease, tissue ulceration, or cardiovascular disease
medicine
-
MMP proteolysis contributes to tissue degeneration and inflammation in osteo and rheumatoid arthritis and may also play a role in the spread of such diseases, abnormally high concentrations of MMPs have been identified in human tissue surrounding invasive carcinomas, indicating a local imbalance in the MMP-TIMP equilibrium which directly enables tumor metastasis through EMP degradation and blood vessel formation
medicine
overexpression of MMps is associated with a variety of diseases ranging from periodontal disease and arthritis to tumor invasion and metastasis
medicine
-
proteolytic activity of the enzyme is precisely regulated by endogenous tissue inhibitors, disruption of this balance results in diseases such as arthritis, atherosclerosis, tumour growth and metastasis
medicine
-
development of natural pharmacological inhibitors of enzyme: Proenzyme is proteolytically activated by plasmin. C18 unsaturated fatty acids are inhibitory, with elaidic acid totally abolishing the activation. Inhibitory effect result from binding of unsaturated fatty acids to kringle 5
medicine
-
significantly higher levels of enzyme, soluble Fas and soluble Fas ligand are found in sera from patients with active untreated adult onset Stills disease compared to healthy control. Serum levels of enzyme, soluble Fas and soluble Fas ligand fluctuate and are parallel to disease activity
medicine
-
no significant elevation in serum levels of enzyme and tissue inhibitor proteinase TIMP-1 of patients with malignant melanoma compared to control. Enzyme levels are significantly different in sera of males and females
medicine
-
enzyme may be involved in the pathogenesis of endometriosis. Endometrial expression of enzyme, matrix metalloproteinases MMP-2 and MMP-11 and tissue inhibitor metalloproteinases TIMP-1 and TIMP-2 are similar in women with endometriosis and in those with peritoneal endometriosis. Expression of enzyme and matrix metalloproteinases MMP-2 and MMP-11 is higher in colorectal endometriosis than in ovarian and peritoneal endometriosis
medicine
-
topical treatment of chronic dermal ulcers
medicine
-
the 5A/6A polymorphism of the MMP3 gene influences arterial remodeling of the common carotid artery in healthy subjects, but not in patients with diabetes mellitus. Therefore, the significance of the 5A/6A polymorphism as a marker of risk in this high cardiovascular risk population seems to be somehow blunted
medicine
-
serum MMP-3 is significantly elevated in ankylosing spondylitis patients with active disease
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
-
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
analysis
Mus musculus Sv129
-
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
-
during gastric ulcer healing, enzyme expression as well as matrix metalloproteinase MMP-2 and MMP-13 are induced in stromal cells of the gastric mucosa bordering the ulcer. Enzyme mRNA is confined to the upper layers of the granulation tissue