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 hide
3.4.24.17
-
RECOMMENDED NAME
GeneOntology No.
stromelysin 1
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
preferential cleavage where P1', P2' and P3' are hydrophobic residues
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
79955-99-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Mus musculus C57B/6J
mouse, C57B/6J
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Manually annotated by BRENDA team
Mus musculus C57BL/6
gene mmp-3
UniProt
Manually annotated by BRENDA team
Mus musculus DBA/1J
DBA/1J mice
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-
Manually annotated by BRENDA team
Sv129 mice
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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despite their similar substrate specificities, the stromelysins show differential patterns of transcriptional regulation and tissue distribution that hint at distinct physiological functions in processes such as skeletal development, wound healing, and vascular remodeling
malfunction
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
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
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-
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(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
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-
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(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
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(7-methoxycoumarin-4-yl)acetyl-P-L-G-L-(L)-2,3-diaminopropionylamide-A-R + H2O
?
show the reaction diagram
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-
?
(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
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(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
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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
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2,4-Dinitrophenyl-Pro-Leu-Gly-Ile-Ala-Gly-Arg-NH2 + H2O
?
show the reaction diagram
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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
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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
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?
Acetyl-Pro-Leu-Gly-thioester-Leu-Leu-Gly ethyl ester + H2O
?
show the reaction diagram
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acetyl-Pro-Leu-Gly-[2-mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5 + H2O
?
show the reaction diagram
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?
Aggrecan core protein + H2O
?
show the reaction diagram
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alpha-Proteinase inhibitor + H2O
2,4-Dinitrophenyl-Pro-Leu-Gly + Ile-Ala-Gly-Arg-NH2
show the reaction diagram
alpha1-Antichymotrypsin + H2O
?
show the reaction diagram
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cleaves at the P1'-P2' bond
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alpha1-antitrypsin + H2O
?
show the reaction diagram
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?
Antithrombin III + H2O
?
show the reaction diagram
-
cleavage of the P1-P1' bond in the reactive center
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Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Nle-NH2 + H2O
?
show the reaction diagram
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Azocoll + H2O
?
show the reaction diagram
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beta-casein + H2O
?
show the reaction diagram
Carboxymethyltransferrin + H2O
?
show the reaction diagram
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cartilage + H2O
?
show the reaction diagram
casein + H2O
?
show the reaction diagram
Collagen type III + H2O
?
show the reaction diagram
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cytosolic protein Apaf-1 + H2O
?
show the reaction diagram
decorin + H2O
transforming growth factor-beta + ?
show the reaction diagram
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?
DQ-collagen I + H2O
?
show the reaction diagram
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?
DQ-collagen IV + H2O
?
show the reaction diagram
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?
Elastin + H2O
?
show the reaction diagram
elastin fELN-125 + H2O
?
show the reaction diagram
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?
fibrin + H2O
fibrin fragments + ?
show the reaction diagram
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?
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
FS-6 + H2O
?
show the reaction diagram
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?
Gelatin + H2O
?
show the reaction diagram
Immunoglobulin G2a + H2O
?
show the reaction diagram
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Laminin + H2O
?
show the reaction diagram
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys (Dnp) + H2O
?
show the reaction diagram
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?
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 + H2O
?
show the reaction diagram
-
fluorogenic substrate
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?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
show the reaction diagram
NFF2 + H2O
?
show the reaction diagram
quenched fluorescence substrate
-
?
osteopontin + H2O
?
show the reaction diagram
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?
pro-caspase-9 + H2O
active caspase-9 + caspase-9 propeptide
show the reaction diagram
Procollagen + H2O
?
show the reaction diagram
triple helical peptide alpha1(V) + H2O
?
show the reaction diagram
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collagen V fibrils
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?
Collagen type IV + H2O
additional information
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cytosolic protein Apaf-1 + H2O
?
show the reaction diagram
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-
?
pro-caspase-9 + H2O
active caspase-9 + caspase-9 propeptide
show the reaction diagram
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activation
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?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
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addition of 5 mM Mn2+ in the presence of Ca2+ restores activity of the apoenzyme, not by Mn2+ alone
additional information
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metalloproteinase
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R,2S)-2-((R)-sec-butyl)-N-hydroxy-3-((4-methoxyphenyl)sulfonyl)cyclopropanecarboxamide
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(1R,3S)-N-hydroxy-2-((4-methoxyphenyl)sulfonyl)-3-((pyridin-3-yloxy)methyl)cyclopropanecarboxamide
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(1R,3S)-N-hydroxy-2-((4-methoxyphenyl)sulfonyl)-3-(5-phenylpentyl)cyclopropanecarboxamide
-
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(2S)-3-(4-fluorophenyl)-N-methyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
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(2S)-3-(benzyloxy)-N-methyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
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(2S)-3-phenyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
(2S)-N-methyl-3-(4-nitrophenyl)-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
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(2S)-N-methyl-3-(pentafluorophenyl)-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
(2S)-N-methyl-3-phenyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
(betaR)-beta-[[[(1S)-1-[[[(1S)-2-methoxy-1-phenylethyl]amino]carbonyl]-2,2-dimethylpropyl]amino]carbonyl]-2-methyl-[1,1'-biphenyl]-4-hexanoic acid
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UK-370106-COOH, potent inhibitor
1,10-phenanthroline
1-([[4-(3,4-dimethylphenoxy)phenyl]sulfonyl]methyl)-N-hydroxy-4-(prop-2-yn-1-yl)cyclohexanecarboxamide
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1-acetyl-N-hydroxy-4-[[4-(phenylsulfanyl)phenyl]sulfonyl]piperidine-4-carboxamide
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1-cyclopropyl-N-hydroxy-4-[(4-phenoxyphenyl)sulfonyl]piperidine-4-carboxamide
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1-cyclopropyl-N-hydroxy-4-[[4-(phenylsulfanyl)phenyl]sulfonyl]piperidine-4-carboxamide
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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
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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
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2(R)-[2-(4'-fluoro-4-biphenylyl)ethyl]-4-(S9-n-butyl-1,5-pentanedioic acid 1)-(alpha(S)-tert-butylglycine methylamide) amide
2-([4-[3'-(2-aminoethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-N-hydroxy-2-methylpropanamide
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2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(3'-trifluoromethyl-biphenyl-4-yl)-hexanoic acid
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2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4'-fluoro-biphenyl-4-yl)-hexanoic acid
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2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4'-trifluoromethyl-biphenyl-4-yl)-hexanoic acid
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2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-naphthalen-1-yl-phenyl)-hexanoic acid
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2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-naphthalen-2-yl-phenyl)-hexanoic acid
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2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-phenethyl-phenyl)-hexanoic acid
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2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-phenoxy-cyclohexa-1,5-dienyl)-hexanoic acid
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2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-propyl-phenyl)-hexanoic acid
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2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-styryl-phenyl)-hexanoic acid
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2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-thiophen-3-yl-phenyl)-hexanoic acid
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2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-phenyl-hexanoic acid
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2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-[4-(1H-indol-2-yl)-phenyl]-hexanoic acid
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2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-[4-(tetrahydro-furan-2-yl)-phenyl]-hexanoic acid
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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
-
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2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(2'-fluoro-biphenyl-4-yl)-hexanoic acid
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2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(2'-sulfamoyl-biphenyl-4-yl)-hexanoic acid
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2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(3'-fluoro-biphenyl-4-yl)-hexanoic acid
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2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-formyl-biphenyl-4-yl)-hexanoic acid
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2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methanesulfinyl-biphenyl-4-yl)-hexanoic acid
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2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methanesulfonyl-biphenyl-4-yl)-hexanoic acid
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2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methoxy-biphenyl-4-yl)-hexanoic acid
-
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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
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2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-[4'-(1H-tetrazol-5-yl)-biphenyl-4-yl]-hexanoic acid
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-
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
-
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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
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-
2-Butyl-6-(4'-cyano-biphenyl-4-yl)-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
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2-Butyl-6-(4-cycloheptyl-phenyl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
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2-Butyl-6-[4'-(N,N-dimethyl-aminooxymethyl)-biphenyl-4-yl]-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
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2-[(2-biphenyl-4-ylethyl)(methyl)sulfamoyl]-N-hydroxyacetamide
-
-
2-[(3-biphenyl-4-ylazetidin-1-yl)sulfonyl]-N-hydroxyacetamide
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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
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2-[[3-(biphenyl-4-yloxy)azetidin-1-yl]sulfonyl]-N-hydroxyacetamide
-
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2-[[4-(2,3'-dimethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
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2-[[4-(2-chlorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
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2-[[4-(2-ethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
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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
-
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2-[[4-(3'-ethyl-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
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3-(4'-cyanobiphenyl-4-yloxy)-N-hydroxypropionamide
-
-
3-(hydroxycarbamoyl)-1-[(4-phenoxybenzoyl)amino]pentyl 2,2-dimethylpropanoate
-
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3-ethyl-N-hydroxy-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethylprolinamide
-
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3-[(4'-cyanobiphenyl-4-yl)oxy]-N-hydroxypropanamide
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3-[(benzyloxy)methyl]-N-hydroxy-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethylprolinamide
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3-[(benzylsulfanyl)methyl]-N-hydroxy-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethylprolinamide
-
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4'-[5-Carboxy-3-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-nonyl]-biphenyl-4-carboxylic acid
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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
-
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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]-N,N-dimethyl-(S)-benzenepropanamide
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
-
-
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
-
-
L-696,418
-
-
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-[(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
-
-
peptide NNGH
-
-
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
sulfonamide-and carbamide substituted piperazine-based MMP inhibitor
-
-
-
TIMP
-
-
-
TIMP-1
TIMP-2
TIMP-3
-
is induced by enamel matrix derivative
-
Tissue inhibitor of metalloproteinases
-
TIMP-1 and TIMP-2
-
tissue inhibitor of metalloproteinases 1
-
TIMP-1, enzyme binding structure analysis and mechanism of inhibition, detailed overview and comparison to stromelysin-2, EC 3.4.24.22
-
tissue inhibitor of metalloproteinases 2
-
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
-
-
-
Z-L-tryptophan
-
inhibits full length stromelysin_1-477 and truncated stromelysin_100-264, enzyme binding structure and kinetics, chemical shift of the carboxylate carbon upon enzyme binding, overview. The tryptophan side chain can bind in the S1 specificity site of stromelysin with the tryptophan alpha carboxylate group coordinated to the active site zinc atom
-
zoledronate
-
-
[dimethylpropanedioato(2-)-kappa2O1,O3][[(methylsulfinyl-kappaS)methyl]phosphonate-kappaO''']platinum
-
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-hematin
-
induces differential autocatalysis of the propeptide
cytosolic protein Apaf-1
-
-
-
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
-
-
-
additional information
-
purified proMMP-3-catalytic domain is activated overnight in the presence of the organomercurial compound 4-aminophenyl mercuric acetate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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 - 1.4
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-norleucine-NH2
additional information
additional information
-
thermodynamic additivity analysis using stromelysin-1 and a series of biphenyl hydroxamate ligands identified through fragment additivity, thermodynamics determined by isothermal titration calorimetry, corrected for proton transfer events, overview. Additivity arises from enthalpic effects, while interaction entropies are unfavorable, the thermodynamic behavior is masked by proton transfer
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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 - 1.35
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Nle-NH2
0.085 - 0.088
beta-casein
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
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
0.00013
peptide NNGH
pH and temperature not specified in the publication
-
0.00000013
tissue inhibitor of metalloproteinases 1
-
catalytic enzyme domain, pH 7.0, 37C
-
0.00000055
tissue inhibitor of metalloproteinases 2
-
catalytic enzyme domain, pH 7.0, 37C
-
0.001 - 0.0188
UK-370106-COCHO
0.0063 - 0.052
Z-L-tryptophan
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
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 hide
LITERATURE
0.000498
-
-
18.6
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
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 - 8.6
-
glomerular basement membrane
6.2
-
azocoll
7
-
assay at
7.2
-
assay at
7.4
-
assay at
7.5 - 7.8
-
-
7.5
-
assay at
7.6
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
subcutaneous and gonadal adipose tissue. Significantly reduced MMP-3 expression in MMP-10-deficient adipose tissues
Manually annotated by BRENDA team
-
from Alzheimer disease patients and controls
Manually annotated by BRENDA team
-
recombinant enzyme
Manually annotated by BRENDA team
-
MMP-3 has been identified in predentin and in dentin, where it localizes within the intertubular dentin, along the collagen fibrils
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
-
the enzyme expression is associated with expression of Rac1b, a tumorigenic splice isoform of Rac1, in all stages of pancreatic cancer, analysis of 140 specimen, overview
Manually annotated by BRENDA team
-
transcriptional profiling, overview
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
-
trophoblatsic cell line
Manually annotated by BRENDA team
-
a human chondrosarcoma cell line
Manually annotated by BRENDA team
-
rheumatoid
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the enzyme moves from cytoplasm to cell nucleus upon Dengue virus infection and colocalizes with NFkappaB P65 in the nucleus
Manually annotated by BRENDA team
the enzyme moves from cytoplasm to cell nucleus upon Dengue virus infection and colocalizes with NFkappaB P65 in the nucleus
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 hide
LITERATURE
24500
-
gel filtration
57000
-
-
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
-
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis of the isolated catalytic enzyme domain in complex with inhibitor TIMP1, PDB ID 1UEA
-
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 hide
LITERATURE
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
10.5
-
more than 80% loss of activity after 15 h
31017
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
15 min, 65% loss of activity of enzyme form HMW, 25% loss of activity of enzyme form LMW
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
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)
-
purified from Escherichia coli
-
recombinant enzyme
-
recombinant His-tagged isolated MMP-3 catalytic domain by nickel affinity chromatography from Escherichia coli
-
recombinant SCD
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catalytic domain expressed in Escherichia coli
-
gene encoding ST1 expressed in lepidopteran Sf9 cells infected with recombinant baculovirus
-
gene mmp-3, quantitative real-time PCR expression analysis
gene MMP3, quantitative RT-PCR enzyme expression analysis, co-expression with GFP-RelA in HEK-293T cells
NF-kappaB and AP-1 are important transcription factors for MMP-3 gene expression. Glycitein inhibits the promoter activitiy of MMP-3, overview
-
recombinant expression of His-tagged isolated MMP-3 catalytic domain as soluble cytoplasmic protein in Escherichia coli
-
recombinant SCD expressed in Escherichia coli
-
selenomethionine-substituted C-terminally truncated proMMP-3(DELTAC) expressed in Escherichia coli B834(DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Curcumin dose dependently suppresses MMP-3 and -9 expression in Helicobacter pylori infected human gastric epithelial cells
-
Curcumin dose dependently suppresses MMP-3 and -9 expression in Helicobacter pylori infected mouse gastric tissues
-
dexamethasone suppression of MMP-3 gene expression
-
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
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
-
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
-
interleukin-1Ra, dexamethasone, and TNF significantly decrease levels of all forms of MMP-3
-
lipopolysaccharide does not induce mmp-3 mRNA expression in peripheral blood samples
MMP-3 expression is upregulated with age, 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
-
MMP-3 is induced in gingival fibroblasts in response to inflammatory cytokines, such as TNF and interleukin-1
-
MMP-3 is upregulated after stroke in brain in the infarcted tissue compared to healthy control areas, overview
-
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
reduced MMP-3 expression in invasive trophoblasts of patients with severe preeclampsia
-
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
-
the expression of the enzyme is upregulated in Dengue virus-infected RAW264.7 cells
TNF-alpha and IL-1beta stimulate production of MMPs through the activation of mitogen-activated protein kinases, NF-kappaB and AP-1
-
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
diagnostics
-
the enzyme, together with gelolin, is a potential biomarker for Alzheimer's disease
medicine