Information on EC 3.4.24.7 - interstitial collagenase and Organism(s) Homo sapiens and UniProt Accession P03956

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Homo sapiens
UNIPROT: P03956


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


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
3.4.24.7
-
RECOMMENDED NAME
GeneOntology No.
interstitial collagenase
CAS REGISTRY NUMBER
COMMENTARY hide
9001-12-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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
2,4-dinitrophenyl-Pro-beta-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(N-methyl-2-aminobenzoyl)-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-Pro-Leu-Ala-Leu-Trp-Ala-Arg-OH + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(dinitrophenyl)-NH2 + H2O
(7-methoxycoumarin-4-yl)-acetyl-Arg-Pro-Lys-Pro-Val-Glu + Nva-Trp-Arg-Lys(dinitrophenyl)-NH2
show the reaction diagram
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-(3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly + Leu-(3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2
show the reaction diagram
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-cyclohexylalanine-Gly-Nve-His-Ala-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-NH2 + H2O
?
show the reaction diagram
-
degradation of synthetic substrate is pH-independent
-
-
?
Ac-Pro-Leu-Gly-SCH2(iBu)CO-Leu-Leu-GlyOEt + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
show the reaction diagram
-
very low activity
-
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
show the reaction diagram
-
-
-
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-OC2H5 + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Pro-Leu-Gly-Leu-Ala-Gly-OC2H5 + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
show the reaction diagram
-
-
-
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-OC2H5 + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
show the reaction diagram
-
very low activity
-
?
acetyl-Pro-Leu-Gly-S-Leu-Leu-Gly ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Pro-Leu-Gly-SCH2[CH2CH(CH3)2CO]-Leu-Leu-OC2H5 + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
show the reaction diagram
-
very low activity
-
?
alpha1(I)772-786 triple-helical peptide + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
casein zymography assay method
-
-
?
Collagen + H2O
?
show the reaction diagram
collagen I + H2O
?
show the reaction diagram
collagen I alpha-1 chain + H2O
?
show the reaction diagram
collagen I alpha-2 chain + H2O
?
show the reaction diagram
GAQGIAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
GLQGIAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Ala-Gly-Gln-Gln
show the reaction diagram
-
-
-
-
?
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Gln-Arg-Gly-Val-Val-Gly-Leu-Hyp-NH2 + H2O
Gly-Pro-Gln-Gly + Ile-Ala-Gly-Gln-Gln-Arg-Gly-Val-Val-Gly-Leu-Hyp-NH2
show the reaction diagram
-
-
-
-
?
GNQGIAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
GNVGLAGA + H2O
?
show the reaction diagram
-
-
-
-
?
GP-Hyp-GIAGA + H2O
?
show the reaction diagram
-
-
-
-
?
GP-Hyp-IAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
GPDGIAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
GPLGIAGP + H2O
?
show the reaction diagram
-
-
-
-
?
GPLGIAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
GPQGIAGA + H2O
?
show the reaction diagram
-
-
-
-
?
GPQGIAGH + H2O
?
show the reaction diagram
-
-
-
-
?
GPQGIAGP + H2O
?
show the reaction diagram
-
-
-
-
?
GPQGIAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
GPQGIAGT + H2O
?
show the reaction diagram
-
-
-
-
?
GPQGLAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
GPRGIAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
GPVGIAGQ + H2O
?
show the reaction diagram
-
-
-
-
?
Human alpha2-macroglobulin + H2O
?
show the reaction diagram
-
cleavage site: Gly679-Leu680
-
-
?
human pregnancy zone protein + H2O
?
show the reaction diagram
-
cleavage sites: Gly685-Leu686, Gly687-Val688, Gly757-Ile758, Ala684-Leu684, and Ala685-Met686
-
-
?
PSYFLNAG + H2O
?
show the reaction diagram
-
-
-
-
?
rat alpha1 macroglobulin + H2O
?
show the reaction diagram
-
cleavage site: His681-Leu682, Phe691-Leu692
-
-
?
rat alpha1-inhibitor 3 (27J) + H2O
?
show the reaction diagram
-
cleavage sites: Ala666-Val667
-
-
?
rat alpha1-inhibitor 3 (2J) + H2O
?
show the reaction diagram
-
cleavage sites: Pro683-Val684
-
-
?
rhodamine 6G-labeled KDP-6-aminohexanoic acid-GPLGIAGIG-6-aminohexanoic acid-PKGY + H2O
rhodamine 6G-labeled KDP-6-aminohexanoic acid-GPLG + IAGIG-6-aminohexanoic acid-PKGY
show the reaction diagram
-
fluorescent biosensor, substrate for matrix metalloproteinases MMP-2, MMP-9, MMP-14
-
-
?
Type I collagen + H2O
?
show the reaction diagram
type I procollagen + H2O
type I collagen + ?
show the reaction diagram
-
-
-
-
?
type II collagen + H2O
?
show the reaction diagram
-
interstitial collagen
-
-
?
type III collagen + H2O
?
show the reaction diagram
[alpha1(I)]2alpha2(I)772-784 triple-helical peptide + H2O
?
show the reaction diagram
-
-
-
-
?
[alpha1(II)769-783] fluorogenic triple-helical peptide-3 + H2O
?
show the reaction diagram
-
-
-
-
?
[alpha1(II)769-783] fluorogenic triple-helical peptide-4 + H2O
?
show the reaction diagram
-
-
-
-
?
[alpha1(II)769-783] single-stranded peptide-3 + H2O
?
show the reaction diagram
-
-
-
-
?
fTHP-3 + H2O
additional information
-
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
collagen I + H2O
?
show the reaction diagram
-
degradation
-
-
?
Type I collagen + H2O
?
show the reaction diagram
type I procollagen + H2O
type I collagen + ?
show the reaction diagram
-
-
-
-
?
type II collagen + H2O
?
show the reaction diagram
-
interstitial collagen
-
-
?
type III collagen + H2O
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
optimum concentration 5 mM
Zn2+
-
in presence of 5 mM Ca2+, optimum concentration 0.001 mM, decrease in activity above
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
epigallocatechin gallate
-
competitive. the galloyl group is important for inhibitory activity
fisetin
-
mixed-type inhibition
pedunculagin
-
potent inhibitory effect on MMP-1 and the increased type-I procollagen synthesis in ultraviolet B-induced human fibroblast
quercetin
-
-
(3-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-phenyl)-carbamic acid tert-butyl ester
-
-
1,10-phenanthroline
2-[benzyl([[(2-methylphenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
-
2-[benzyl([[(4-chlorophenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
-
2-[benzyl([[(4-fluorophenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
-
2-[benzyl([[(4-methylphenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
-
3-[((1R,4S)-7,7-Dimethyl-2-oxo-bicyclo[2.2.1]hept-1-ylmethanesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(2,4-Dinitro-phenylsulfanyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(2,5-Dichloro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(2-Hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-benzoic acid
-
-
3-[(3-Chloro-4-ethylamino-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(3-Chloro-4-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(4-Bromo-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(4-Chloro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(4-Fluoro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(5-Dimethylamino-naphthalene-1-sulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(Heptadecachlorooctane-1-sulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[3-(2,4-Dichloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-(3,4-Dichloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-(3-Chloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-(4-Chloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-(4-Chloro-phenylsulfonyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-(4-Fluoro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-(4-Fluoro-phenylsulfonyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-Benzoyl-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[Benzenesulfonyl-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[[3-[3-(4-chloro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
-
3-[[3-[3-(4-fluoro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
-
3-[[4-[3-(4-chloro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
-
3-[[4-[3-(4-fluoro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
-
4-[(2-Hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-benzoic acid
-
-
Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
-
pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
alpha2-Macroglobulin
-
-
-
C3H7-POOH-Ile-Trp-NHMe
-
phosphonamidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
ClCH2CO-(N-OH)Leu-Ala-Gly-NH2
-
2-5 mM, 25C, pH 7.4, Tris buffer, strong irreversible inhibition, inhibition increases with higher temperatures and inhibitor concentration
ClCH2CO-(N-OH)Phe-Ala-Ala-NH2
-
-
CT 1746
-
-
-
dexamethasone
-
significantly decreases active MMP-1 level and inhibits active MMP-1
disodium isostearyl 2-O-L-ascorbyl phosphate
-
i.e. disodium 2-(1,3,3-trimethyl-n-butyl)-5,7,7-trimethyl-n-octyl-L-ascorbyl phosphate or VCP-IS-2Na, an amphiphilic vitamin C derivative, increases proliferation of normal human skin fibroblasts, NHDFs and NB1RGBs, by 123% and 135% and inhibits MMP-1 production by a maximum of 19% and 11% in NHDF and NB1RGB cells at 0.05 mM, respectively
dithiothreitol
-
-
epigallocatechin-3-gallate
-
-
EtO-POOH-CH2-Leu-Trp-NHMe
-
pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
EtO-POOH-Ile-Ala-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
EtO-POOH-Ile-Ala-Gly-Gln-Arg-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
EtO-POOH-Ile-Ala-Gly-Glu-Arg(NO2)-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
EtO-POOH-Ile-Ala-Gly-Glu-Arg-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
EtO-POOH-Ile-Leu-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
EtO-POOH-Ile-Trp-NHMe
-
phosphoramidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
EtO-POOH-Ile-Tyr(OBzl)-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
EtO-POOH-Ile-Tyr-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
exopolysaccharide
-
obtained from mycelial culture of Grifola frondosa HB0071 may contribute to inhibitory action in photoaging skin by reducing the MMP-1-related matrix degradation system
-
GM6001
-
a broad-spectrum MMP inhibitor
hexyl-POOH-CH2-Leu-Trp-NHMe
-
pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
hexyl-POOH-Leu-Trp-NHMe
-
pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
hexyl-POOH-O-Leu-Trp-NHMe
-
pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
N-2-methylphenylsulfonylureido-N-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-2-methylphenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-2-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-2-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-2-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-4-chlorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-4-chlorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine
-
-
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
-
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-4-fluorophenylsulfonylureido-N-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-4-fluorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-4-fluorophenylsulfonylureido-N-[(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
-
N-4-fluorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-4-fluorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
-
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-4-methylphenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-4-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-4-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-Hydroxy-3-[(2-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(3-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-iodo-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-methoxy-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(2,4,6-trimethyl-benzenesulfonyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(2-nitro-phenylsulfanyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(3-trifluoromethyl-benzenesulfonyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(4-nitro-phenylsulfanyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(nonachlorobutane-1-sulfonyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(quinoline-8-sulfonyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(toluene-4-sulfonyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-pentafluorobenzenesulfonyl-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-phenylmethanesulfonyl-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-trichloromethanesulfonyl-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-trifluoromethanesulfonyl-amino]-propionamide
-
-
N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-o-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-p-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
-
N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-phenylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
-
N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-o-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
-
N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-p-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
-
N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-phenylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
-
N-Hydroxy-3-[(naphthalene-1-sulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(naphthalene-2-sulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[1-(4-nitro-benzyl)-3-o-tolylsulfonyl-ureido]-propionamide
-
-
N-Hydroxy-3-[1-(4-nitro-benzyl)-3-p-tolylsulfonyl-ureido]-propionamide
-
-
N-Hydroxy-3-[1-(4-nitro-benzyl)-3-phenylsulfonyl-ureido]-propionamide
-
-
N-Hydroxy-3-[dimethylsulfamoyl-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[methanesulfonyl-(4-nitro-benzyl)-amino]-propionamide
-
-
N-phenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-phenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-phenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
naphthoyl-Gly-PSI[POOHCH2]-Leu-Trp-NHBzl
-
pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
PAI-1
-
functions as an upstream regulator of a MMP-1-initiated collagenolytic phenotype, it blocks conversion of MMP-1 to its active form. Neutralization of endogenous PAI-1 with function blocking antibodies accelerates both collagenolysis and activation of MMP-1
-
phthaloyl-Gly(P)-Ile-Trp-(R)NHCH-(Me)Ph
-
phosphonamidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
phthaloyl-Gly(P)-Ile-Trp-NHBzl
-
50 M, 25C, pH 7.4, Tris buffer, reversible inhibition, protects the enzyme partially from inactivation by ClCH2CO-(N-OH)Leu-Ala-Gly-NH2
phthaloyl-Gly-PSI[POOHNH]-Ile-Trp-(S)NHCH-(Me)Ph
-
phosphonamidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
Ro-31-9790
-
-
TIMP-1
-
TIMP-2
-
TIMP-3
-
is induced by enamel matrix derivative
-
tissue inhibitor of matrix metalloproteinase-1
-
is not influenced by substance P
-
tissue inhibitor of matrix metalloproteinase-2
-
0.1 microM, inhibits both protease activity and migration in a 3-dimensional cross-linked collagen matrix
-
Tissue inhibitor of metalloproteinase-1
-
TIMP-1
-
tissue inhibitors of metalloproteinase-1
-
i.e. TIMP-1
-
TVGCEECTV
-
-
[3-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-phenyl]-carbamic acid tert-butyl ester
-
-
-
[4-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-phenyl]-carbamic acid tert-butyl ester
-
-
-
[5-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-2-methoxy-phenyl]-carbamic acid tert-butyl ester
-
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15-deoxy-DELTA12,14-prostaglandin J2
-
treatment of with 30 mM of 15-deoxy-DELTA12,14-prostaglandin J2 increases the expression of heme oxygenase-1, which precedes the induction of matrix metalloproteinases. The 15-deoxy-DELTA12,14-prostaglandin J2-induced upregulation of MMP-1 is abrogated by the heme oxygenase-1 inhibitor zinc protoporphyrin IX as well as introduction of heme oxygenase-1 short interfering RNA
4-aminophenylmercuric acetate
-
MMP-1 from synovial fibroblasts is activated with 10 mM 4-aminophenylmercuric acetate in 0.1 N NaOH at 37 C for 3 h
glucose
-
presence of high glucose levels and interferon gamma in culture medium have a synergistic effect on the expression of matrix metalloproteinases MMP-1, MMP-9 and interleukin-1beta. High glucose also enhances interferon gamma-induced priming effect on lipopolysaccharide-stimulated MMP-1 secretion. High glucose and interferon gamma exert the synergistic effect on MMP-1 expression by enhancing STAT1 phosphorylation and STAT1 transcriptional activity
interferon gamma
-
presence of high glucose levels and interferon gamma in culture medium have a synergistic effect on the expression of matrix metalloproteinases MMP-1, MMP-9 and interleukin-1beta. High glucose also enhances interferon gamma-induced priming effect on lipopolysaccharide-stimulated MMP-1 secretion. High glucose and interferon gamma exert the synergistic effect on MMP-1 expression by enhancing STAT1 phosphorylation and STAT1 transcriptional activity
-
interleukin-1 receptor antagonist
-
increases active MMP-1 level
-
TNF
-
increases active MMP-1 level
-
Trypsin
-
procollagenase activated to collagenase
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013
2,4-dinitrophenyl-Pro-beta-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(N-methyl-2-aminobenzoyl)-NH2
-
pH 7.5, 40C
0.026
2,4-dinitrophenyl-Pro-Leu-Ala-Leu-Trp-Ala-Arg-OH
-
pH 7.5, 25C
0.0013
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-OC2H5
-
-
0.0012
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-OC2H5
-
-
0.0039
acetyl-Pro-Leu-Gly-SCH[CH2CH(CH3)2CO]-Leu-Leu-OC2H5
-
-
-
0.063 - 0.2076
alpha1(I)772-786 triple-helical peptide
-
0.00000000086 - 0.00000074
collagen I alpha-1 chain
-
0.00000000025 - 0.00000053
collagen I alpha-2 chain
-
0.0612 - 0.0666
fTHP-3
-
3.3
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Gln
-
wild-type enzyme
0.63
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Gln-Arg-Gly-Val-Val-Gly-Leu-Hyp-NH2
-
wild-type enzyme
3.6
GPLGIAGQ
-
-
3.6
GPQGIAGA
-
-
3.3
GPQGIAGQ
-
-
2.4
GPQGIAGT
-
-
2.8
GPQGLAGQ
-
-
5.6
GPRGIAGQ
-
-
4.9
GPVGIAGQ
-
-
0.0008
human type I collagen
-
-
-
0.0021
human type II collagen
-
-
-
0.0013
human type III collagen
-
-
-
0.8
type I collagen
-
-
-
0.0013
type III collagen
-
pH 7.5, 25C, wild-type substrate
-
0.0037
[alpha1(I)]2alpha2(I)772-784 triple-helical peptide
-
mutant enzyme E200A
-
0.0612
[alpha1(II)769-783] fluorogenic triple-helical peptide-3
-
wild-type enzyme
-
0.0208
[alpha1(II)769-783] fluorogenic triple-helical peptide-4
-
wild-type enzyme
-
0.171
[alpha1(II)769-783] single-stranded peptide-3
-
wild-type enzyme
-
additional information
additional information
-
kinetics with wild-type and mutant FG-5015 I785P type III collagen substrates, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.3
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-OC2H5
-
-
5.83
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-OC2H5
-
-
103
acetyl-Pro-Leu-Gly-SCH[CH2CH(CH3)2CO]-Leu-Leu-OC2H5
-
-
-
0.11 - 0.28
alpha1(I)772-786 triple-helical peptide
-
0.21 - 10.41
collagen I alpha-1 chain
-
0.014 - 58.61
collagen I alpha-2 chain
-
0.08 - 0.087
fTHP-3
-
0.2
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Gln
-
wild-type enzyme
0.51
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Gln-Arg-Gly-Val-Val-Gly-Leu-Hyp-NH2
-
wild-type enzyme
0.333
GPLGIAGQ
-
-
0.217
GPQGIAGA
-
-
0.203
GPQGIAGQ
-
-
0.263
GPQGIAGT
-
-
0.27
GPQGLAGQ
-
-
0.0717
GPRGIAGQ
-
-
0.15
GPVGIAGQ
-
-
0.0148
human type I collagen
-
-
-
0.000267
human type II collagen
-
-
-
0.0056 - 0.153
human type III collagen
-
0.00278
type I collagen
-
-
-
0.077
type III collagen
-
pH 7.5, 25C, wild-type substrate
-
0.08
[alpha1(II)769-783] fluorogenic triple-helical peptide-3
-
wild-type enzyme
-
0.04
[alpha1(II)769-783] fluorogenic triple-helical peptide-4
-
wild-type enzyme
-
0.25
[alpha1(II)769-783] single-stranded peptide-3
-
wild-type enzyme
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
880000 - 630000000
collagen I alpha-1 chain
-
1200000 - 1900000000
collagen I alpha-2 chain
-
58
type III collagen
-
pH 7.5, 25C, wild-type substrate
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0105
epigallocatechin gallate
-
pH 7.5, 25C
0.00135
fisetin
-
pH 7.5, 40C
0.00149
quercetin
-
pH 7.5, 40C
0.00002
(3-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-phenyl)-carbamic acid tert-butyl ester
-
-
0.000162
2-[benzyl([[(2-methylphenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
pH 6.0, 37C
0.000143
2-[benzyl([[(4-chlorophenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
pH 6.0, 37C
0.000135
2-[benzyl([[(4-fluorophenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
pH 6.0, 37C
0.00017
2-[benzyl([[(4-methylphenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
pH 6.0, 37C
0.000057
3-[((1R,4S)-7,7-Dimethyl-2-oxo-bicyclo[2.2.1]hept-1-ylmethanesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000027
3-[(2,4-Dinitro-phenylsulfanyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.00005
3-[(2,5-Dichloro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000031
3-[(2-Hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-benzoic acid
-
-
0.00005
3-[(3-Chloro-4-ethylamino-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.00003
3-[(3-Chloro-4-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000024
3-[(4-Bromo-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000023
3-[(4-Chloro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000021
3-[(4-Fluoro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000089
3-[(5-Dimethylamino-naphthalene-1-sulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000077
3-[(Heptadecachlorooctane-1-sulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000018
3-[3-(2,4-Dichloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000036
3-[3-(3,4-Dichloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000026
3-[3-(3-Chloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000024
3-[3-(4-Chloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.00004
3-[3-(4-Chloro-phenylsulfonyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000021
3-[3-(4-Fluoro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000047
3-[3-(4-Fluoro-phenylsulfonyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000032
3-[3-Benzoyl-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000025
3-[Benzenesulfonyl-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000057
3-[[3-[3-(4-chloro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
-
0.000055
3-[[3-[3-(4-fluoro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
-
0.000056
3-[[4-[3-(4-chloro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
-
0.000055
3-[[4-[3-(4-fluoro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
-
0.00003
4-[(2-Hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-benzoic acid
-
-
0.002
C3H7-POOH-Ile-Trp-NHMe
-
phosphonamidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
0.5
ClCH2CO-(N-OH)Leu-Ala-Gly-NH2
-
25C, pH 7.4, Tris buffer
2.5
ClCH2CO-(N-OH)Phe-Ala-Ala-NH2
-
25C, pH 7.4, Tris buffer
0.0000128 - 0.0000603
CT 1746
-
0.004
EtO-POOH-CH2-Leu-Trp-NHMe
-
pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
0.12
EtO-POOH-Ile-Ala-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
0.5
EtO-POOH-Ile-Ala-Gly-Gln-Arg-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
0.27
EtO-POOH-Ile-Ala-Gly-Glu-Arg(NO2)-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
0.4
EtO-POOH-Ile-Ala-Gly-Glu-Arg-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
0.045
EtO-POOH-Ile-Leu-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
0.012
EtO-POOH-Ile-Trp-NHMe
-
phosphoramidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
0.002
EtO-POOH-Ile-Tyr(OBzl)-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
0.02
EtO-POOH-Ile-Tyr-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
0.3
hexyl-POOH-O-Leu-Trp-NHMe
-
pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
0.000039
N-2-methylphenylsulfonylureido-N-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37C
0.000036
N-2-methylphenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37C
0.000038
N-2-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37C
0.000029
N-2-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37C
0.000015
N-2-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37C
0.000024
N-4-chlorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37C
0.000024
N-4-chlorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37C
0.00019
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine
-
pH 6.0, 37C
0.00002
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37C
0.00023
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
pH 6.0, 37C
0.000014
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37C
0.000025
N-4-fluorophenylsulfonylureido-N-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37C
0.000021
N-4-fluorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37C
0.0002
N-4-fluorophenylsulfonylureido-N-[(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
pH 6.0, 37C
0.000021
N-4-fluorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37C
0.000013
N-4-fluorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37C
0.000017
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37C
0.00018
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
pH 6.0, 37C
0.000011
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37C
0.000032
N-4-methylphenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37C
0.00003
N-4-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37C
0.000018
N-4-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37C
0.000024
N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37C
0.000015
N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37C
0.000043
N-Hydroxy-3-[(2-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.00005
N-Hydroxy-3-[(3-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000032
N-Hydroxy-3-[(4-iodo-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000023
N-Hydroxy-3-[(4-methoxy-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.00005
N-Hydroxy-3-[(4-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000035
N-Hydroxy-3-[(4-nitro-benzyl)-(2,4,6-trimethyl-benzenesulfonyl)-amino]-propionamide
-
-
0.000028
N-Hydroxy-3-[(4-nitro-benzyl)-(2-nitro-phenylsulfanyl)-amino]-propionamide
-
-
0.000006
N-Hydroxy-3-[(4-nitro-benzyl)-(3-trifluoromethyl-benzenesulfonyl)-amino]-propionamide
-
-
0.000024
N-Hydroxy-3-[(4-nitro-benzyl)-(4-nitro-phenylsulfanyl)-amino]-propionamide
-
-
0.000069
N-Hydroxy-3-[(4-nitro-benzyl)-(nonachlorobutane-1-sulfonyl)-amino]-propionamide
-
-
0.000055
N-Hydroxy-3-[(4-nitro-benzyl)-(quinoline-8-sulfonyl)-amino]-propionamide
-
-
0.00003
N-Hydroxy-3-[(4-nitro-benzyl)-(toluene-4-sulfonyl)-amino]-propionamide
-
-
0.000002
N-Hydroxy-3-[(4-nitro-benzyl)-pentafluorobenzenesulfonyl-amino]-propionamide
-
-
0.000027
N-Hydroxy-3-[(4-nitro-benzyl)-phenylmethanesulfonyl-amino]-propionamide
-
-
0.000023
N-Hydroxy-3-[(4-nitro-benzyl)-trichloromethanesulfonyl-amino]-propionamide
-
-
0.000022
N-Hydroxy-3-[(4-nitro-benzyl)-trifluoromethanesulfonyl-amino]-propionamide
-
-
0.000055
N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-o-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
0.00005
N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-p-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
-
0.000062
N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-phenylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
-
0.00007
N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-o-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
-
0.000057
N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-p-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
-
0.000069
N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-phenylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
-
0.000082
N-Hydroxy-3-[(naphthalene-1-sulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000065
N-Hydroxy-3-[(naphthalene-2-sulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000069
N-Hydroxy-3-[1-(4-nitro-benzyl)-3-o-tolylsulfonyl-ureido]-propionamide
-
-
0.000042
N-Hydroxy-3-[1-(4-nitro-benzyl)-3-p-tolylsulfonyl-ureido]-propionamide
-
-
0.000052
N-Hydroxy-3-[1-(4-nitro-benzyl)-3-phenylsulfonyl-ureido]-propionamide
-
-
0.000038
N-Hydroxy-3-[dimethylsulfamoyl-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000087
N-Hydroxy-3-[methanesulfonyl-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000025
N-phenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37C
0.000015
N-phenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37C
0.000013
N-phenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37C
0.002
phthaloyl-Gly-PSI[POOHNH]-Ile-Trp-(S)NHCH-(Me)Ph
-
phosphonamidate inhibitor, pH 6.5, 25 C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
0.0000108 - 0.0001893
Ro31-9790
0.00005
[4-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-phenyl]-carbamic acid tert-butyl ester
-
-
-
0.000024
[5-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-2-methoxy-phenyl]-carbamic acid tert-butyl ester
-
-
-
additional information
additional information
-
Ki-values above 250 nM are determined for N-4-fluorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine, N-4-chlorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine, N-phenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine, N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine, N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine, N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine, N-4-fluorophenylsulfonylureido-N-(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine, N-4-chlorophenylsulfonylureido-N-(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine, N-4-methylphenylsulfonylureido-N-[(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine, N-4-fluorophenylsulfonylureido-N-[(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014
epigallocatechin gallate
Homo sapiens
-
pH 7.5, 25C
0.00975
pedunculagin
Homo sapiens
-
pH 7.5, 20C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
-
-
6.5 - 7.5
-
-
7 - 8
-
skin
7 - 9
-
bone
7.4
-
assay at
7.5 - 8.5
-
-
7.5
-
assay at
7.6
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.2
-
degradation of collagen I: at pH 7.5 a 10fold higher activity is observed toward the alpha-2 chain, whereas a very similar value for the two chains is detected at pH 7.0. At pH lower 7.0 the overall enzymatic activity toward the alpha-1 chain increases, whereas the processing of the alpha-2 chain remains essentially constant between pH 7.3 and 6.0; degradation of collagen I: over the whole pH range investigated the proteolytic activity on the alpha2 chains is higher than for the alpha1 chain. Difference is large at alkaline pH (40fold at pH 9.2) and it decreases as the pH decreases toward the physiological value where the enzymatic processing of the alpha2 chain is only 4times higher than for the alpha1 chain. Difference remains essentially unchanged down to pH 6.3; degradation of synthetic substrate is pH-independent; degradation of synthetic substrate: overall enzymatic activity of ect-MMP-14 displays a pH dependence characterized by maximum efficiency at pH 7.0, which decreases upon both pH increase and pH decrease
6.5 - 9.5
-
pH 6.5: about 65% of maximal activity, pH 9.5: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
MMP-1 is upregulated by TGF-beta, EGF and IL-1beta
Manually annotated by BRENDA team
-
cell line JJ, increased MMP1 expression in chondrosarcoma, mechanism, overview
Manually annotated by BRENDA team
-
mucosa, immunohistochemic analysis of MMP-1 and TIMP-1 levels, overview. Overall plasma levels of MMP-1 and TIMP-1 in ulcerative colitis patients are significantly higher than those of the control group
Manually annotated by BRENDA team
-
acceleration of matrix metalloproteinase-1 production by oxidized low-sensity lipoprotein and 4-hydroxynonenal
Manually annotated by BRENDA team
-
MMP-1 is expressed by migrating enterocytes bordering intestinal ulcers. In the fetal gut model, MMP-1 expression by migrating enterocytes is detected
Manually annotated by BRENDA team
-
primary epithelial ovarian tumor cell
Manually annotated by BRENDA team
-
MMP-14 is expressed and active in cultured ES2 cells. ES2 cells also exhibit MMP-dependent invasion of and proliferation within three-dimensional collagen gels
Manually annotated by BRENDA team
-
immortalized human keratinocyte cells
Manually annotated by BRENDA team
-
MMP-10 and MMP-1 are up-regulated in HaCaT II-4 cells
Manually annotated by BRENDA team
-
glycine-extended gastrin renders colon cancer cells more invasive by increasing MMP-I expression via the putative glycine-extended gastrin receptor
Manually annotated by BRENDA team
-
primary, monocyte-derived
Manually annotated by BRENDA team
-
high MMP-1 level
Manually annotated by BRENDA team
-
Muller glia cell line
Manually annotated by BRENDA team
-
saphenous vein smooth muscle
Manually annotated by BRENDA team
-
UM1 and UM2 are oral tongue squamous cell carcinoma cell lines
Manually annotated by BRENDA team
-
ovarian clear cell carcinoma cell
Manually annotated by BRENDA team
-
enzyme expression is significantly stronger in the epithelium than in the stroma
Manually annotated by BRENDA team
-
the mean salivary MMP-1 concentration in patients with chronic periodontitis is significantly higher before and after treatment with aprotinin, as compared to healthy subjects
Manually annotated by BRENDA team
-
disruption of caveolae by addition of methyl-beta-cyclodextrin results in a dramatic decline in both motility and invasion abilities of cells with concomitant increase in secreted MMP-2 expression and expression levels of MMP-1 and MMP-9
Manually annotated by BRENDA team
-
disruption of caveolae by addition of methyl-beta-cyclodextrin results in a dramatic decline in both motility and invasion abilities of cells with concomitant increase in secreted MMP-2 expression and expression levels of MMP-1 and MMP-9
Manually annotated by BRENDA team
-
SCL-1 cell. MMP-1 is upregulated 4 h after UVA and 16 h after UVB irradiation of tumor cells. Incubation of cells with the MEK1/2 inhibitor U0126 or the p38 inhibitor SB202190 abolishes the UVA and UVB mediated induction of MMP-1
Manually annotated by BRENDA team
-
a human chondrosarcoma cell line
Manually annotated by BRENDA team
-
rheumatoid
Manually annotated by BRENDA team
-
fibroblast-like, from rheumatoid arthritis patients
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
leg ulcer tissue from patients with chronic venous insufficiency
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
intracellular association of MMP-1 to mitochondria and nuclei confers resistance to apoptosis and may explain the association of this enzyme with tumor cell survival and spreading
Manually annotated by BRENDA team
-
intracellular association of MMP-1 to mitochondria and nuclei confers resistance to apoptosis and may explain the association of this enzyme with tumor cell survival and spreading
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21000
-
x * 21000, SDS-PAGE
38000
-
gel filtration
50000
-
x * 50000, exon 5 mutant species, SDS-PAGE
51929
-
x * 51929, the minor glycosylated enzyme form has a MW of 57000 Da, calculation from nucleotide sequence
53000
-
calculated
58000
-
x * 58000, N-glycosylated exon 5 mutant species, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 21000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
small angle X-ray scattering
-
hanging drop vapour-diffusion method. Crystal structure of the active form of human MMP-1 at 2.67 A resolution. This is a MMP-1 structure that is free of inhibitor and a water molecule essential for peptide hydrolysis is observed coordinated with the active site zinc
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type and exon 5 mutant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain BL21(DE3)
-
expression in Escherichia coli
-
expression analysis
-
expression analysis of MMP1 in cancerous and healthy oral tissues, overview
-
integrity of MMP-1 promoter AP-1 binding site is necessary for transactivation by rapamycin, regulation, overview
-
MMP-3/MMP-1 chimeras and variants are overexpressed in Escherichia coli, folded from inclusion bodies and isolated as zymogens
-
quantitative MMP-1 expression analysis
-
quantitative MMP-1 expression analysis in primary dermal fibroblasts
-
quantitative MMP-1 expression analysis in skin fibroblasts
-
quantitative MMP-1 expression analysis, overview
-
quantitiative real-time PCR expression analysis of MMP-1 in brain regions in response to infection with Mycobacterium tuberculosis
-
sitting drop vapor diffusion technique. Crystallization of recombinant human proMMP-1 and determination of its structure to 2.2 A resolution
-
the enzyme forms insoluble inclusion bodies when over-expressed in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activation of toll-like receptors TLR2, TLR3 or TLR5 increased the expression of MMP-1. MMP-1 and MMP-9 in human epidermal keratinocytes are induced by Pam3CSK4, Poly(I:C) and flagellin, which are ligands for TLR2, TLR3 and TLR5, respectively, overview. The induction of MMP-1 by the receptor ligands is inhibited by pretreatment with BAY11-7082, a NF-kappaB inhibitor, or SP600125, a JNK inhibitor. p38 MAPK activation negatively regulates MMP-1 induction by TLR2 or TLR5 activation, but not by TLR3 activation
-
bortezomib specifically increases the steady-state mRNA levels of MMP-1 and enhances the binding of c-Jun to the promoter of MMP-1. Disruption of the proximal AP-1-binding site in the promoter of MMP-1 severely impairs MMP-1 transcription in response to bortezomib. By altering the binding of at least two transcription factors, c-Jun and SP1, proteasome inhibition results in increased production of MMP-1 and decreases synthesis of type I collagen in human dermal fibroblasts
-
both the MMP-1 and TIMP-1 mRNA expression level are dramatically downregulated by baicalin
-
curcumin at the concentration of 2.5-5 mg/ml specifically downregulates MMP-1 mRNA in BT-483 and MDA-MB-231 breast cancer cell lines. Cell growth and proliferation is inhibited in presence of curcumin, overview
-
curcumin, a potent inhibitor for AP-1, or simvastatin inhibit the expression of MMP-1. Suppression of c-Jun expression by RNA interference significantly inhibits MMP-1 expression
-
dexamethasone suppression of MMP-1 gene expression
-
dexamethasone, and less potent also interleukin-1Ra and TNF, decrease levels of pro-MMP-1
-
enhanced collagen degradation, in case of epithelial-to-mesenchymal transition stimulated by transforming growth factor-beta as well as epidermal growth factor receptor, is coupled to a significant increase in matrix metalloproteinase MMP-1 expression and is involved a proteolytic axis composed of plasmin, MMP-10, ec 3.4.24.22, and MMP-1
-
expression of MMP-1 in cartilages and synovial tissues is suppressed by the treatment of curcumin and indomethacin. Production of MMP-1 is inhibited by curcumin in tumor necrosis factor-alpha-stimulated rheumatoid arthritis fibroblast-like synoviocytes and chondrocytes in a dose-dependent manner putatively through the inhibition of PKCdelta and the JNK/c-Jun signaling pathway, overview
-
expression of MMP-1 is markedly increased by both onion extract and quercetin in vitro in human skin fibroblasts
-
fucoidan treatment significantly inhibits the expression of MMP-1
-
hypoxia and specifically HIF-1a increase CXCR4, its ligand SDF1, and MMP1 expressions in JJ cell line and chondrosarcoma invasion in vitro, which can be inhibited by siRNA directed at HIF-1a or CXCR4, the CXCR4 inhibitor AMD3100, as well as with ERK inhibitor U0126 and ERK siRNA. Hypoxia increases MMP1 mRNA expression 9fold which is further increased to 23fold by SDF1 stimulation
-
increased MMP1 expression in JJ cell line can be inhibited by siRNA directed at HIF-1a or CXCR4, the CXCR4 inhibitor AMD3100, as well as with ERK inhibitor U0126 and ERK siRNA
-
induction of MMP-1 by UV-A irradiation treatment of cultured human dermal fibroblasts
-
inhibition of MMP-1 expression by extracts of Kaempferia pandurata, overview
-
inhibtitory effects of potent antioxidant astaxanthin on the MMP-1 induction by UV-A irradiation, overview
-
interleukin-6, high glucose, and lipopolysaccharide act in concert and synergistically upregulate MMP-1 expression by U-937 mononuclear phagocytes via ERK1/2 and JNK pathways and c-Jun, mechanism, overview. c-Jun is a key subunit of AP-1 known to be essential for MMP-1 transcription
-
lithium specifically induces a rapid and pronounced up-regulation of MMP-1 at the mRNA and protein levels, whereas the induction of two the other senescent cell markers plasminogen activator inhibitor-1 and interleukin-8 is either delayed or weak, respectively. Lithium affects MMP-1 expression mainly at the transcriptional level but neither the AP1/Ets regulatory sites nor the redox sensitive -1607/2G site in MMP-1 promoter are involved in lithium-dependent MMP-1 regulation
-
matrix metalloproteinase-1 expression is induced by interleukin-1beta requiring acid sphingomyelinase, overview
-
MMP-1 expression and secretion is induced by infection with Mycobacterium tuberculosis by 57.8%, the specific inhibitor TIMP-1 expression is also induced by 243.7%. The MMP-1 induction is specifically inhibited by 4-aminosalicyclic acid via inhibiting a p38 MAPK-prostaglandin signaling cascade, overview
-
MMP-1 expression is induced by UV-B irradiation, the induction is inhibited by extracts of Kaempferia pandurata, as are phosphorylation of MAP kinases ERK, JNK, and p38, overview
-
MMP-1 is 4.1fold induced by infection with Mycobacterium tuberculosis. Conditioned medium from Mycobacterium tuberculosis-infected human monocytes stimulates greater MMP-1 gene expression in human microglial cells than direct infection, overview. The induction is suppressed by dexamethasone. TNF-alpha and interleukin-1beta are necessary but not sufficient for upregulating MMP-1 secretion. NF-kappaB and AP-1 c-Jun/FosB heterodimers regulate induction of MMP-1 secretion by conditioned medium from Mycobacterium tuberculosis and are upregulated in granulomas from patients with cerebral tuberculosis. CoMTb upregulates MMP-1 gene expression and secretion in microglia
-
MMP-1 is downregulated 4fold during trophoblast differentiation, reduced MMP-1 expression in pre-eclampsia and fetal growth restriction
-
MMP-1 is induced in gingival fibroblasts in response to inflammatory cytokines, such as TNF and interleukin-1. TNF treatment of human gingival fibroblasts significantly induces the expression of MMP-1 severalfold, while enamel matrix derivative alone has no effect
-
MMP-1 is upregulated after stroke in brain in the infarcted tissue compared to healthy control areas, overview
-
phorbol 12-myristate 13-acetate and interleukin-1beta significantly stimulate the production of MMP-1 by periodontal ligament cells at both the transcriptional and the translational level
-
Rac1 inhibitor NSC23766 suppresses MMP1 in dermal fibroblasts, and half-lives of type I collagen protein are increased
-
recombinantly overexpressed RhoB enhances migration and MMP1 expression of prostate cancer DU145 cells, overview
-
SB203580 and PD98059 suppress MMP-1 secretion
-
TNF-alpha and IL-1beta stimulate production of MMPs through the activation of mitogen-activated protein kinases, NF-kappaB and AP-1
-
UV-B irradiation induces MMP-1 expression and secretion. Inhibitory effects of Costaria costata fucoidan on UVB-induced MMP-1 promoter, mRNA, and protein expression in vitro by 41.8% at 10 ng/ml, 57.7% at 100 ng/ml, and 70% at 0.001 mg/ml compared to UV-B irradiation alone, overview
-
UVA and UVB irradiation of dermal fibroblasts in vitro or human skin in vivo induces MMP-1 expression. MMP-1 expression and secretion induced by UV-B irradiation is inhibited by trans-zeatin, a cytokinin from Zea mays, and by PD98059, an ERK inhibitor, by SP600125, a JNK inhibitor and by SB203580, a p38 MAPK inhibitor. trans-Zeatin also inhibits UVB-induced ERK, JNK, p38 MAPK and c-Jun phosphorylation
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E219A
-
inactive mutant
V94G
-
constitutively active MMP-1 mutant. Expression of MMP-1 V94G in young skin in organ culture causes fragmentation and ultrastructural alterations of collagen fibrils similar to those observed in aged human skin in vivo. Expression of MMP-1 V94G in dermal fibroblasts cultured in three-dimensional collagen lattices causes substantial collagen fragmentation, which is markedly reduced by MMP-1 siRNA-mediated knockdown or MMP inhibitor MMI270. Fibroblasts cultured in MMP-1 V94G-fragmented collagen lattices display many alterations observed in fibroblasts in aged human skin, including reduced cytoplasmic area, disassembled actin cytoskeleton, impaired TGF-beta pathway, and reduced collagen production
DELTA243-340
-
about 10% increase in turnover number and 9% increase in Km-value compared to wild-type enzyme with fTHP-3 as substrate
DELTA243-450
-
the KM-value for the alpa1(I)772-786 triple-helical peptide is 3.3fold higher than that of the wild-type enzyme, the turnover number for this substrate is 2.5fold higher
R183Q/W184W/T185T/N186K/N187D/F188T/R189T/E190G/Y191T
-
mutation reduces collagenolytic activity about 10fold
Y191T
-
mutation reduces collagenolytic and gelatinolytic activity about 5fold
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
optimal folding occurs when the denatured protein is diluted at 4C in 2 M guanidine HCl, 20% glycerol, 2.5 mM reduced and oxidized glutathione, 5 mM CaCl2, followed by buffer exchange to remove denaturant and thiols
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
synthesis
-
improved method for high-level expression of soluble human MMP-1 catalytic domain in Escherichia coli
analysis
-
detection of localized extracellular sites of protease activity by use of fluorescent biosensor rhodamine 6G-labeled KDP-6-aminohexanoic acid-GPLGIAGIG-6-aminohexanoic acid-PKGY. Protease activity is localized at the polarized leading edge of migrating tumor cells rather than further back on the cell body. The path of proteolytic cleavage by a migrating cell can be visualized in 2- and 3-dimensional matrices. Probe can be used to determine inhibitor concentrations needed to suppress cell-surface protease activity
diagnostics
medicine
pharmacology
-
MMP-1 is a potential target in therapy of melanoma