Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
((Gly-Pro-4-hydroxyproline)5-Gly-Pro-Lys(7-methoxycoumarin-4-yl) acetyl)-Gly-Pro-Gln-Gly-Cys(4-methoxybenzyl)-Arg-Gly-Gln-Lys(2,4-dinitrophenyl)-Gly-Val-Arg-(Gly-Pro-4-hydroxyproline)5-NH2 + H2O
?
triple-helical substrate fTHP-9
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-L-Lys-Pro-Leu-Gly-Leu-Lys(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Ala-Cys(p-OmeBz)-Trp-Ala-Arg(Dpa)-NH2 + H2O
?
-
-
-
-
?
(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
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Tyr-Ala-Nva-Trp-Met-Lys-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-GTQGQEARGS-dinitrophenol NH2 + H2O
?
substrate covering the aggrecanase cleavage site of aggrecan
-
-
?
(7-methoxycoumarin-4-yl)acetyl-L-Pro-Leu-Gly-Leu-(3-[2,4-dinitrophenyl]-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-LAQAVRSSK-dinitrophenol NH2 + H2O
?
quenched fluorescent substrate mimicking the cleavage site of pro tumor necrosis factor alpha
-
-
?
(7-methoxycoumarin-4-yl)acetyl-P-3-cyclohexylalanyl-norvalyl-HA-dinitrophenol NH2 + H2O
?
collagenase substrate
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-cyclohexylalanine-Gly-norvaline-His-Ala-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-NH2 + H2O
?
-
degradation of synthetic substrate is pH-independent
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Ala-Cys(p-OMeBz)-Trp-Ala-Arg(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Ala-Gln-Ala-Val-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Arg-Ser-Ser-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Ala-Nva-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 + H2O
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Lys-Pro-Leu-Ala-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2 + H2O
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly + Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
triple-helical substrate fTHP-9
-
-
?
alpha subunit of low density lipoprotein receptor-related protein + H2O
?
-
-
-
-
?
alpha-1 microglobulin + H2O
?
-
-
-
-
?
alpha-2 macroglobulin + H2O
?
-
-
-
-
?
alpha-2-HS-glycoprotein + H2O
?
-
-
-
-
?
alpha1-antitrypsin + H2O
?
alpha1-proteinase inhibitor + H2O
?
-
-
-
-
?
alpha2-macroglobulin + H2O
?
-
-
-
-
?
alpha5 integrin + H2O
?
-
-
-
-
?
apolipoprotein A-I + H2O
?
-
-
-
-
?
apolipoprotein A-IV + H2O
?
-
-
-
-
?
apolipoprotein J + H2O
?
-
-
-
-
?
betaglycan + H2O
?
-
-
-
-
?
brain-specific angiogenesis inhibitor 1 + H2O
vasculostatin-120 + vasculostatin-40
-
the N terminus of BAI1 is cleaved extracellularly to generate a truncated receptor (vasculostatin-120) and a 40000 Da fragment (vasculostatin-40)
-
-
?
CCN3 + H2O
CPPQCPGR + DGQIGCVPR + KVEVPGECCEK + KPVMVIGTCTCHTNCPK + ?
-
-
-
?
collagen I alpha-1 chain + H2O
?
-
overall enzymatic activity is higher on the alpha-2 chain for both MMP-1 and MMP-2. In MMP-2 a marked difference for substrate affinity (higher for the alpha-1 chain) is overwhelmed by an even more marked propensity to cleave the alpha-2 chain
-
-
?
collagen I alpha-2 chain + H2O
?
-
overall enzymatic activity is higher on the alpha-2 chain for both MMP-1 and MMP-2. In MMP-2 a marked difference for substrate affinity (higher for the alpha-1 chain) is overwhelmed by an even more marked propensity to cleave the alpha-2 chain
-
-
?
collagen type I alpha-1 chain + H2O
?
-
the MMP-14 ectodomain preferentially cleaves the alpha-1 chain of collagen type I
-
-
?
collagen type I alpha-2 chain + H2O
?
-
-
-
-
?
complement component 3 + H2O
?
-
-
-
-
?
cross-linked fibrin II + H2O
?
des-fibrinopeptides A and B, prepared by clotting fibrinogen with thrombin in the presence of factor XIIIa
-
-
?
dabcyl-Gly-Gly-Pro-Gln-Gly-Ile-Trp-Gly-Gln-Lys(fluorescein)-Ahx-Cys + H2O
?
-
-
-
?
dermatan sulfate proteoglycan + H2O
?
-
-
-
?
endoglin + H2O
soluble endoglin + ?
-
MMP-14 cleaves membrane-bound endoglin at a site in close proximity to the transmembrane domain between Gly586-Leu-587
-
-
?
entactin + H2O
?
-
-
-
-
?
epidermal growth factor receptor + H2O
?
-
the enzyme plays a role in transactivation
-
-
?
extracellular matrix metalloproteinase inducer + H2O
?
-
-
-
-
?
extracellular matrix metalloproteinase inducer + H2O
extracellular matrix metalloproteinase inducer fragment + ?
-
-
22000 Da in length
-
?
F-gelatin + H2O
?
-
-
-
?
fibrillin + H2O
?
-
-
-
-
?
fibroblast growth factor receptor-1 + H2O
?
-
-
-
?
fibroblast growth factor receptor-4 + H2O
?
-
-
-
?
galectin-3
?
-
cleaved to the 22 kDa degradation product when exposed to cells expressing membrane-anhored wild type MT1-MMP or the recombinant 50 kDa enzyme form
-
-
?
gelsolin + H2O
?
-
-
-
-
?
growth differentiation factor-1 + H2O
?
-
-
-
?
heparin-binding epidermal growth factor + H2O
?
heparin-binding epidermal growth factor + H2O
heparin-binding epidermal growth factor mN3-fragment + ?
-
-
-
-
?
hepatocyte growth factor activator inhibitor-1 + H2O
?
inactive pro-matrix metalloproteinase-2 + H2O
active matrix metalloproteinase-2 + ?
-
-
-
-
?
inter-alpha inhibitor H4 + H2O
?
-
-
-
-
?
intercellular cell adhesion molecule-1 + H2O
?
-
-
-
-
?
kidney injury molecule-1 + H2O
?
the enzyme cleaves and sheds the substrate's ectodomain
-
-
?
KiSS-1/metastin + H2O
?
-
-
-
-
?
laminin-5 + H2O
?
-
-
-
?
laminin-5 beta3 chain + H2O
?
-
-
-
-
?
mannose-binding lectin + H2O
?
-
-
-
-
?
MCP-3/CCL7 + H2O
?
-
-
-
-
?
membrane-bound Semaphorin 4D + H2O
soluble Semaphorin 4D + ?
-
-
-
-
?
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2 + H2O
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly + Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
-
-
-
?
MOCAcPLGLA2pr-dinitrophenol-A-RNH2 + H2O
?
fluorogenic substrate
-
-
?
N-cadherin + H2O
?
-
-
-
-
?
N-hexanoyl((GP-4-hydroxy-L-proline)5GPK(7-methoxycoumarin-4-yl)acetyl)GPQGLRGQK(2,4-dinitrophenyl)GVR(GP-4-hydroxy-L-proline)5-NH2 + H2O
N-hexanoyl((GP-4-hydroxy-L-proline)5GPK(7-methoxycoumarin-4-yl)acetyl)GPQGL + RGQK(2,4-dinitrophenyl)GVR(GP-4-hydroxy-L-proline)5-NH2
-
-
-
-
?
neuronal glial antigen 2 + H2O
?
three (210, 160, and 51-52 kDa) major cleavage products are formed
-
-
?
PA83
?
-
efficiently cleaved by MT1-MMP at the substrate-enzyme ratio as low as 1: 50
-
-
?
peptide IAG + H2O
?
enzyme binding structure, modelling, overview
-
-
?
pericentrin + H2O
?
-
-
-
-
?
pro-alpha v integrin + H2O
?
-
-
-
?
pro-alpha5 integrin subunit + H2O
?
-
-
-
-
?
pro-alpha5beta3 integrin subunit + H2O
?
-
-
-
-
?
pro-matrix metalloproteinase-13 + H2O
?
-
activation
-
-
?
pro-matrix metalloproteinase-8 + H2O
?
-
activation
-
-
?
pro-MMP-2
?
-
MT1-MMP accomplishes full pro-MMP-2 activation, cleavage within the prodomain at the Asn37-Leu38 peptide bond
-
-
?
pro-MMP-2 + H2O
mature MMP-12 + MMP-2 pro-peptide
pro-MMP-2 + H2O
MMP-2 + ?
-
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
pro-MMP-2 + H2O
MMP-2 + propeptide
-
-
-
?
pro-MMP2 + H2O
MMP-2 + ?
-
activation in the presence of TIMP-2
-
-
?
pro-tissue necrosis factor alpha + H2O
?
-
-
-
-
?
pro-transforming growth factor beta + H2O
?
-
-
-
-
?
progelatinase A + H2O
gelatinase A + ?
-
activation, gelatinase A is matrix metalloproteinase-2
-
-
?
progelatinase A E375A + H2O
?
syn: pro-matrix metalloproteinase 2, cleaves at N37-L38 only
-
-
?
proMMP-13 + H2O
?
-
activation
-
-
?
proMMP-2 + H2O
MMP-2 + ?
-
activation
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
proMMP-2 + H2O
MMP-2 + pro-peptide
proMMP-8 + H2O
?
-
activation
-
-
?
rat-tail tendon type I collagen + H2O
?
-
degraded by deltaTM-MT1-MMP at 37ưC
-
-
?
receptor of complement component 1q + H2O
?
cleaves at Gly79-Gln80, cleavage with CAT/PEX domain leads to fragments with the following MW: 17 kDa, 12 kDa and 11 kDa
-
-
?
receptor-activator of NF-kB ligand + H2O
?
-
-
-
-
?
recombinant mutated aggrecan fusion protein 1 + H2O
?
-
-
-
?
SDF-1/CXCL12 + H2O
?
-
-
-
-
?
stromal cell-derived factor 1 + H2O
?
-
-
-
?
syndecan + H2O
?
-
-
-
-
?
syndecan-1 core protein + H2O
?
syndecan-1 G245L glutathione transferase protein + H2O
?
cleaves at G82-L83 peptide bond
-
-
?
testican-1 + H2O
?
-
-
-
-
?
tissue transglutaminase + H2O
?
-
-
-
-
?
transforming growth factor-beta + H2O
?
-
-
-
?
type 1 collagen + H2O
?
-
-
-
-
?
type I collagen + H2O
denatured type I collagen
-
bound by recombinant linker/hemopexin C domain of MT1-MMP
-
-
?
type I collagen chain alpha-1 + H2O
?
-
-
-
-
?
type I collagen chain alpha-2 + H2O
?
-
-
-
-
?
type III collagen + H2O
?
type-I collagen + H2O
?
-
-
-
-
?
additional information
?
-
(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 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
fluorescent peptide
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
-
fluorescent peptide
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
-
cdMT1-MMP is catalytically more efficient towards small peptide substrates than deltaTM-MT1-MMP and the haemopexin domain of MT1-MMP facilitates the hydrolysis of triple-helical substrates
-
-
?
aggrecan + H2O

?
-
-
-
-
?
aggrecan + H2O
?
recombinant fusion protein with G332A mutation, substrate is cleaved at the aggrecanase site in its interglobular domain sequence segment, products are fragments with the following MW: 72 kDa, 66 kDA and 42 kDa
-
-
?
alpha1-antitrypsin + H2O

?
-
-
-
-
?
alpha1-antitrypsin + H2O
?
-
-
-
?
apolipoprotein E + H2O

?
-
-
-
-
?
apolipoprotein E + H2O
?
-
the 34 kDa apoE protein is initially processed by MMP-14 into fragments with molecular masses of 28, 23, 21, and 11 kDa. The primary MMP-14 cleavage sites are Ala176-Ile177, Pro183-Leu184, Pro202-Leu203, and Gln249-Ile250. The MMP-14-mediated cleavage of apoE is consistent regardless of whether apoE exists in its lipid-bound or lipid-free form. Upon digestion with MMP-14, apoE loses its ability to suppress the platelet-derived growth factor-induced migration of rat vascular smooth muscle cells
-
-
?
CCN5 + H2O

?
-
-
-
?
CCN5 + H2O
?
UniProt ID O76076, CCN5 lacks the CTCK domain
-
-
?
CD44 + H2O

?
-
-
-
-
?
Collagen + H2O

?
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
collagen I + H2O

?
-
-
-
?
collagen I + H2O
?
-
degradation
-
-
?
collagen I + H2O
?
-
degradation, substrate from rat tail
-
-
?
collagen I + H2O
?
-
degradation
-
-
?
E-cadherin + H2O

?
-
-
-
-
?
E-cadherin + H2O
?
-
MT1-MMP sheds E-cadherin at cell-cell adherens junctions
-
-
?
Fibrinogen + H2O

?
-
-
-
-
?
Fibrinogen + H2O
?
-
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
-
alpha, beta and gamma chains
-
-
?
Fibronectin + H2O

?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
cell surface active pMMP-2 cDNAs bound to MT1-MMP enhances substrate digestion, cytoplasmic tail of MT1-MMP not required for digestion
-
-
?
Gelatin + H2O

?
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
poor activity
-
-
?
Gelatin + H2O
?
-
rat-tail tendon type I collagen boiled for 5 min and denatured to gelatin, when degraded by deltaTM-MT1-MMP and cdMT1-MMP
-
-
?
Gelatin + H2O
?
-
-
-
-
?
heparin-binding epidermal growth factor + H2O

?
-
the enzyme removes the NH2-terminal 20 amino acids by cleaving between A-83LC
-
-
?
heparin-binding epidermal growth factor + H2O
?
-
the enzyme removes the NH2-terminal 20 amino acids by cleaving between A-83LC
-
-
?
hepatocyte growth factor activator inhibitor-1 + H2O

?
-
-
-
?
hepatocyte growth factor activator inhibitor-1 + H2O
?
the 66 kDa protein is cleaved to 58, 42, and 16 kDa fragments
-
-
?
Laminin + H2O

?
-
-
-
-
?
Laminin-1 + H2O

?
-
-
-
-
?
Laminin-1 + H2O
?
-
-
-
?
pro-MMP-2 + H2O

?
-
-
-
?
pro-MMP-2 + H2O
?
-
MT-MMP1 activates MMP-2, EC 3.4.24.24
-
-
?
pro-MMP-2 + H2O

mature MMP-12 + MMP-2 pro-peptide
-
-
-
-
?
pro-MMP-2 + H2O
mature MMP-12 + MMP-2 pro-peptide
-
activation of MMP-2
-
-
?
pro-MMP-2 + H2O

MMP-2 + MMP-2 propeptide
-
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
MMP14 is essential for proMMP-2 activation: pro-MMP-2 activation by MMP14/TIMP complex is realized in an environment of low TIMP concentration
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
the TIMP-2-dependent pathway of MMP-2 activation involves tissue inhibitor of MMP-2 as a bridging molecule between MT1-MMP and pro-MMP-2. Thus, net activity of MT1-MMP and MMP-2 is regulated in a complex manner depending on TIMP-2 concentration. For the TIMP-2-independent pathway, claudin recruits MT-MMP and MMP-2 at a tight junction to achieve elevated focal concentrations, and consequently enhances activation of pro-MMP-2. Pro-MMP-2 associates with TIMP-2-deficient cells through the hemopexin domain, and is processed by MT2-MMP
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
pro-MMP-2 is cleaved by an adjacent TIMP-2-free MT1-MMP between Asn37 and Leu38, generating an activated intermediate form that is further processed to the fully activated form by an intermolecular auto-cleavage when an intermediate form is present at a sufficiently high concentration at the cell surface, mechanism, overview. MT1-MMP cannot cleave other direct substrates at the TIMP-2 level that induces efficient pro-MMP-2 processing
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
the TIMP-2-dependent pathway of MMP-2 activation involves tissue inhibitor of MMP (TIMP)-2 as a bridging molecule between MT1-MMP and pro-MMP-2. Thus, net activity of MT1-MMP and MMP-2 is regulated in a complex manner depending on TIMP-2 concentration. For the TIMP-2-independent pathway, claudin recruits MT-MMP and MMP-2 at a tight junction to achieve elevated focal concentrations, and consequently enhances activation of pro-MMP-2. Pro-MMP-2 associates with TIMP-2-deficient cells through the hemopexin domain, and is processed by MT2-MMP
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
pro-MMP-2 is cleaved by an adjacent TIMP-2-free MT1-MMP between Asn37 and Leu38, generating an activated intermediate form that is further processed to the fully activated form by an intermolecular auto-cleavage when an intermediate form is present at a sufficiently high concentration at the cell surface, mechanism, overview. MT1-MMP cannot cleave other direct substrates at the TIMP-2 level that induces efficient pro-MMP-2 processing
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
?
progelatinase A + H2O

?
-
-
-
?
progelatinase A + H2O
?
syn: pro-matrix metalloproteinase 2, leads to activation of progelatinase A
-
-
?
progelatinase A + H2O
?
-
syn: pro-matrix metalloproteinase 2, leads to activation of progelatinase A
-
-
?
progelatinase A + H2O
?
syn: pro-matrix metalloproteinase 2, leads to activation of progelatinase A
-
-
?
progelatinase A + H2O
?
-
syn: pro-matrix metalloproteinase 2, leads to activation of progelatinase A
-
-
?
progelatinase A + H2O
?
syn: pro-matrix metalloproteinase 2, leads to activation of progelatinase A
-
-
?
progelatinase A + H2O
?
cleaves at N37-L38 and N80-Y81
-
-
?
progelatinase A + H2O
?
21 kDa fragment
-
-
?
progelatinase A + H2O
?
-
-
-
-
?
proMMP-2 + H2O

?
-
-
-
-
?
proMMP-2 + H2O
?
-
activation
-
-
?
proMMP-2 + H2O
?
-
activation
-
-
?
proMMP-2 + H2O

MMP-2 + MMP-2 pro-peptide
-
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
-
-
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
-
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
-
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
activation
-
-
?
proMMP-2 + H2O

MMP-2 + pro-peptide
-
-
-
?
proMMP-2 + H2O
MMP-2 + pro-peptide
-
-
-
-
?
syndecan-1 + H2O

?
-
-
-
-
?
syndecan-1 + H2O
?
-
-
-
?
syndecan-1 core protein + H2O

?
-
-
-
-
?
syndecan-1 core protein + H2O
?
cleaves preferably at G245-L246 peptide bond
-
-
?
transglutaminase + H2O

?
-
-
-
-
?
transglutaminase + H2O
?
tissue transglutaminase that binds fibronectin
-
-
?
Type I collagen + H2O

?
-
-
-
-
?
Type I collagen + H2O
?
-
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
Type I collagen + H2O
?
-
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
Type I collagen + H2O
?
-
-
-
?
Type I collagen + H2O
?
-
cleavage of collagen by MT1-MMP regulates cell growth and invasion in a collagen-rich environment
-
-
?
Type I collagen + H2O
?
-
type I collagen binds MT1-MMP via a hemopexin-like domain and is cleaved
-
-
?
type II collagen + H2O

?
-
-
-
-
?
type II collagen + H2O
?
-
-
-
?
type III collagen + H2O

?
-
-
-
-
?
type III collagen + H2O
?
-
-
-
?
Vitronectin + H2O

?
-
-
-
-
?
Vitronectin + H2O
?
-
-
-
?
additional information

?
-
degrades extracellular matrix compounds
-
-
?
additional information
?
-
-
membrane type 1 matrix metalloproteinase activates progelatinase A, a type IV collagenase, on the cell surface of tumors. Membrane type 1-matrix metalloproteinase may play an important role in the invasive growth and spread of breast cancer cells by specifically activating pro-MMP-2 to cleave the connective-tissue barrier
-
-
?
additional information
?
-
breakdown of extracellular matrix
-
-
?
additional information
?
-
-
breakdown of extracellular matrix
-
-
?
additional information
?
-
breakdown of extracellular matrix
-
-
?
additional information
?
-
involved in cell migration
-
-
?
additional information
?
-
involved in cell migration
-
-
?
additional information
?
-
-
involved in cell migration
-
-
?
additional information
?
-
involved in cell migration
-
-
?
additional information
?
-
-
involved in cell migration
-
-
?
additional information
?
-
involved in cell migration
-
-
?
additional information
?
-
enzyme activates gelatinase
-
-
?
additional information
?
-
-
enzyme activates gelatinase
-
-
?
additional information
?
-
role in extracellular matrix remodelling under physiological and pathological conditions
-
-
?
additional information
?
-
degrades components of tissue barriers, regulates cell-extracellular matrix interaction by processing cell adhesion molecules such as CD44 and integrin alpha v chain
-
-
?
additional information
?
-
-
degrades components of tissue barriers, regulates cell-extracellular matrix interaction by processing cell adhesion molecules such as CD44 and integrin alpha v chain
-
-
?
additional information
?
-
remodeling of the extracellular matrix
-
-
?
additional information
?
-
central role in tumor cell invasion
-
-
?
additional information
?
-
central role in tumor cell invasion
-
-
?
additional information
?
-
-
central role in tumor cell invasion
-
-
?
additional information
?
-
key protease in tumor cell invasion
-
-
?
additional information
?
-
-
the enzyme regulates extracellular matrix remodeling and is capable of cleaving a wide variety of transmembrane proteins. The enzymatic activity of MT1-MMP is regulated by endogenous inhibitors, TIMP, the tissue inhibitor of metalloproteinases
-
-
?
additional information
?
-
-
hydrolysis of triple helical substrates that, via addition of N-terminal alkyl chains, differ in their thermal stabilities, substitution of Cys(4-methoxybenzyl) for Leu in the P1' subsite is greatly favored by MMP-14, increase in substrate triple-helical thermal stability leads to the decreased ability of the enzyme to cleave such substrates
-
-
?
additional information
?
-
-
rat-tail tendon type I collagen not degraded by cdMT1-MMP at 37ưC
-
-
?
additional information
?
-
-
MT1-MMP plays an important role in early cancer dissemination by converting epithelial cells to migratory mesenchymal-like cells
-
-
?
additional information
?
-
-
pro-alpha2 integrin subunit is not a substrate
-
-
?
additional information
?
-
-
enzyme regulation, transcription factor EGR1 is involved, overview
-
-
?
additional information
?
-
the enzyme performs autoproteolysis
-
-
?
additional information
?
-
-
membrane-type MMPs are membrane spanning binding sites that play an important role in the cell surface activation of MMPs such as MMP-2
-
-
?
additional information
?
-
-
MT1-MMP on cell surface rapidly turns over by auto-degradation or clathrin-dependent internalization. MT1-MMP inactivated by TIMP-2 avoids auto-degradation, and accumulates on the cell surface, overview. Tetraspanins are attracting attention as binding proteins of MT1-MMP, which regulate subcellular localization and compartmentalization of MT1-MMP and consequent MT1-MMP activities
-
-
?
additional information
?
-
-
overview of MT1-MMP-associating proteins by localization and MT1-MMP-associating membrane proteins by function. Some proteins, such as MT1-SP, EGFR, 5T4, DCP, and CD36L1, preferentially precipitate pro-MT1-MMP, other proteins, e.g. GA733-1, HAI-1, HAI-2, TF, THBD, and CD9, precipitate preferentially the active form of MT1-MMP indicating that these proteins may form a complex on the cell surface
-
-
?
additional information
?
-
-
membrane proteins were cleaved by MT1-MMP in a MMI270-sensitive manner
-
-
?
additional information
?
-
the enzyme does not degrade fibroblast growth factor-2 or fibroblast growth factor receptor-2
-
-
?
additional information
?
-
interaction analysis of MMP14 with proteins in HeLa cells identified by inactive catalytic domain capture yeast 2-hybrid analysis, overview. Detection of CCN5 as a MMP14 substrate by yeast 2-hybrid screening
-
-
?
additional information
?
-
CCN = cysteine rich protein 61/connective tissue growth factor/nephroblastoma overexpressed
-
-
?
additional information
?
-
modeling of enzyme-substrate interaction
-
-
?
additional information
?
-
-
modeling of enzyme-substrate interaction
-
-
?
additional information
?
-
-
healing process
-
-
?
additional information
?
-
-
in vivo growth of FaDu cells co-injected with murine fibroblasts is increased, while their progression is reduced in MT1-MMP-deficient fibroblasts, overview
-
-
?
additional information
?
-
-
MT1-MMP on cell surface rapidly turns over by auto-degradation or clathrin-dependent internalization. MT1-MMP inactivated by TIMP-2 avoids auto-degradation, and accumulates on the cell surface, overview. Tetraspanins are attracting attention as binding proteins of MT1-MMP, which regulate subcellular localization and compartmentalization of MT1-MMP and consequent MT1-MMP activities
-
-
?
additional information
?
-
-
MT1-MMP activates MMP-2
-
-
?
additional information
?
-
-
MT1-MMP is increased in myocardial ischemia and reperfusion, and contributes to myocardial dysfunction, upstream induction mechanism by release of endothelin and protein kinase C activation, microdialysis analysis, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CCN5 + H2O
?
UniProt ID O76076, CCN5 lacks the CTCK domain
-
-
?
fibroblast growth factor receptor-1 + H2O
?
-
-
-
?
fibroblast growth factor receptor-4 + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
growth differentiation factor-1 + H2O
?
-
-
-
?
hepatocyte growth factor activator inhibitor-1 + H2O
?
kidney injury molecule-1 + H2O
?
the enzyme cleaves and sheds the substrate's ectodomain
-
-
?
Laminin-1 + H2O
?
-
-
-
?
laminin-5 + H2O
?
-
-
-
?
neuronal glial antigen 2 + H2O
?
three (210, 160, and 51-52 kDa) major cleavage products are formed
-
-
?
pro-MMP-2 + H2O
?
-
MT-MMP1 activates MMP-2, EC 3.4.24.24
-
-
?
pro-MMP-2 + H2O
mature MMP-12 + MMP-2 pro-peptide
-
activation of MMP-2
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
pro-MMP-2 + H2O
MMP-2 + propeptide
-
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
proMMP-2 + H2O
MMP-2 + pro-peptide
stromal cell-derived factor 1 + H2O
?
-
-
-
?
syndecan-1 + H2O
?
-
-
-
?
transforming growth factor-beta + H2O
?
-
-
-
?
Vitronectin + H2O
?
-
-
-
?
additional information
?
-
Collagen + H2O

?
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
collagen I + H2O

?
-
-
-
?
collagen I + H2O
?
-
degradation
-
-
?
collagen I + H2O
?
-
degradation
-
-
?
Gelatin + H2O

?
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
hepatocyte growth factor activator inhibitor-1 + H2O

?
-
-
-
?
hepatocyte growth factor activator inhibitor-1 + H2O
?
the 66 kDa protein is cleaved to 58, 42, and 16 kDa fragments
-
-
?
pro-MMP-2 + H2O

MMP-2 + MMP-2 propeptide
-
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
MMP14 is essential for proMMP-2 activation: pro-MMP-2 activation by MMP14/TIMP complex is realized in an environment of low TIMP concentration
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
the TIMP-2-dependent pathway of MMP-2 activation involves tissue inhibitor of MMP-2 as a bridging molecule between MT1-MMP and pro-MMP-2. Thus, net activity of MT1-MMP and MMP-2 is regulated in a complex manner depending on TIMP-2 concentration. For the TIMP-2-independent pathway, claudin recruits MT-MMP and MMP-2 at a tight junction to achieve elevated focal concentrations, and consequently enhances activation of pro-MMP-2. Pro-MMP-2 associates with TIMP-2-deficient cells through the hemopexin domain, and is processed by MT2-MMP
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
the TIMP-2-dependent pathway of MMP-2 activation involves tissue inhibitor of MMP (TIMP)-2 as a bridging molecule between MT1-MMP and pro-MMP-2. Thus, net activity of MT1-MMP and MMP-2 is regulated in a complex manner depending on TIMP-2 concentration. For the TIMP-2-independent pathway, claudin recruits MT-MMP and MMP-2 at a tight junction to achieve elevated focal concentrations, and consequently enhances activation of pro-MMP-2. Pro-MMP-2 associates with TIMP-2-deficient cells through the hemopexin domain, and is processed by MT2-MMP
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
-
-
?
proMMP-2 + H2O

MMP-2 + MMP-2 pro-peptide
-
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
-
-
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
-
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
-
-
-
?
proMMP-2 + H2O
MMP-2 + MMP-2 pro-peptide
activation
-
-
?
proMMP-2 + H2O

MMP-2 + pro-peptide
-
-
-
?
proMMP-2 + H2O
MMP-2 + pro-peptide
-
-
-
-
?
Type I collagen + H2O

?
-
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
Type I collagen + H2O
?
-
-
-
?
Type I collagen + H2O
?
-
cleavage of collagen by MT1-MMP regulates cell growth and invasion in a collagen-rich environment
-
-
?
additional information

?
-
-
membrane type 1 matrix metalloproteinase activates progelatinase A, a type IV collagenase, on the cell surface of tumors. Membrane type 1-matrix metalloproteinase may play an important role in the invasive growth and spread of breast cancer cells by specifically activating pro-MMP-2 to cleave the connective-tissue barrier
-
-
?
additional information
?
-
breakdown of extracellular matrix
-
-
?
additional information
?
-
-
breakdown of extracellular matrix
-
-
?
additional information
?
-
breakdown of extracellular matrix
-
-
?
additional information
?
-
involved in cell migration
-
-
?
additional information
?
-
involved in cell migration
-
-
?
additional information
?
-
-
involved in cell migration
-
-
?
additional information
?
-
involved in cell migration
-
-
?
additional information
?
-
-
involved in cell migration
-
-
?
additional information
?
-
involved in cell migration
-
-
?
additional information
?
-
enzyme activates gelatinase
-
-
?
additional information
?
-
-
enzyme activates gelatinase
-
-
?
additional information
?
-
role in extracellular matrix remodelling under physiological and pathological conditions
-
-
?
additional information
?
-
degrades components of tissue barriers, regulates cell-extracellular matrix interaction by processing cell adhesion molecules such as CD44 and integrin alpha v chain
-
-
?
additional information
?
-
-
degrades components of tissue barriers, regulates cell-extracellular matrix interaction by processing cell adhesion molecules such as CD44 and integrin alpha v chain
-
-
?
additional information
?
-
remodeling of the extracellular matrix
-
-
?
additional information
?
-
central role in tumor cell invasion
-
-
?
additional information
?
-
central role in tumor cell invasion
-
-
?
additional information
?
-
-
central role in tumor cell invasion
-
-
?
additional information
?
-
key protease in tumor cell invasion
-
-
?
additional information
?
-
-
the enzyme regulates extracellular matrix remodeling and is capable of cleaving a wide variety of transmembrane proteins. The enzymatic activity of MT1-MMP is regulated by endogenous inhibitors, TIMP, the tissue inhibitor of metalloproteinases
-
-
?
additional information
?
-
-
enzyme regulation, transcription factor EGR1 is involved, overview
-
-
?
additional information
?
-
-
membrane-type MMPs are membrane spanning binding sites that play an important role in the cell surface activation of MMPs such as MMP-2
-
-
?
additional information
?
-
-
MT1-MMP on cell surface rapidly turns over by auto-degradation or clathrin-dependent internalization. MT1-MMP inactivated by TIMP-2 avoids auto-degradation, and accumulates on the cell surface, overview. Tetraspanins are attracting attention as binding proteins of MT1-MMP, which regulate subcellular localization and compartmentalization of MT1-MMP and consequent MT1-MMP activities
-
-
?
additional information
?
-
-
overview of MT1-MMP-associating proteins by localization and MT1-MMP-associating membrane proteins by function. Some proteins, such as MT1-SP, EGFR, 5T4, DCP, and CD36L1, preferentially precipitate pro-MT1-MMP, other proteins, e.g. GA733-1, HAI-1, HAI-2, TF, THBD, and CD9, precipitate preferentially the active form of MT1-MMP indicating that these proteins may form a complex on the cell surface
-
-
?
additional information
?
-
the enzyme does not degrade fibroblast growth factor-2 or fibroblast growth factor receptor-2
-
-
?
additional information
?
-
interaction analysis of MMP14 with proteins in HeLa cells identified by inactive catalytic domain capture yeast 2-hybrid analysis, overview. Detection of CCN5 as a MMP14 substrate by yeast 2-hybrid screening
-
-
?
additional information
?
-
-
healing process
-
-
?
additional information
?
-
-
in vivo growth of FaDu cells co-injected with murine fibroblasts is increased, while their progression is reduced in MT1-MMP-deficient fibroblasts, overview
-
-
?
additional information
?
-
-
MT1-MMP on cell surface rapidly turns over by auto-degradation or clathrin-dependent internalization. MT1-MMP inactivated by TIMP-2 avoids auto-degradation, and accumulates on the cell surface, overview. Tetraspanins are attracting attention as binding proteins of MT1-MMP, which regulate subcellular localization and compartmentalization of MT1-MMP and consequent MT1-MMP activities
-
-
?
additional information
?
-
-
MT1-MMP activates MMP-2
-
-
?
additional information
?
-
-
MT1-MMP is increased in myocardial ischemia and reperfusion, and contributes to myocardial dysfunction, upstream induction mechanism by release of endothelin and protein kinase C activation, microdialysis analysis, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2R)-4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-N-hydroxy-2-[[(4'-methoxybiphenyl-4-yl)sulfonyl](propan-2-yloxy)amino]butanamide
-
(2R)-4-(acetylamino)-2-[(biphenyl-4-ylsulfonyl)amino]-N-hydroxybutanamide
-
1-cyclopropyl-N-hydroxy-4-[(4-[4-[4-(trifluoromethyl)phenyl]piperazin-1-yl]phenyl)sulfonyl]piperidine-4-carboxamide
-
-
4-([4-[4-(2-chlorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-([4-[4-(2-fluorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-([4-[4-(4-chlorophenyl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
AB815
-
against hinge region of MT1-MMP
-
Acetohydroxamic acid
inhibition of Co2+-MT1-MMP
AG3340
-
inhibits MT1-MMP in a sub-nanomolar range
alpha1-PDX
-
completely abats MT1-MMP-induced gelatin degradation by A375 cells
-
alpha1-PIMT1
-
alpha1-proteinase inhibitor-based inhibitor by incorporating the MT1-MMP propeptide sequence into the alpha1-PI reactive-site loop, inhibits proMT1-MMP activation
-
alpha1-PIPDX
-
alpha1-proteinase inhibitor-based inhibitor with furin consensus cleavage sequence inserted into the reactive-site loop, inhibits proMT1-MMP activation
-
anti-membrane-type 1-MMP antibody
-
antibodies LEM-1 and LEM-2 inhibit endothelial cell invasion in a dose dependent manner
-
bone marrow stromal cell antigen 2
best-2, interaction with MT1-MMP via the cytoplasmic tails of both. Bst-2 inhibits the release of virus from infectious cells and this inhibition can be reversed by MT1-MMP. Bst-2 tetherin activity is blocked by MT1-MMP
-
CT1399
-
inhibits endothelial cell invasion
-
CT1847
-
inhibits endothelial cell invasion
-
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
furin inhibitor repressing activation of MMP-2
DX2400
human monoclonal antibody
-
EDTA
-
10 mM, non-specific inhibitor
epigallocatechin-3-gallate
-
-
genistein
-
markedly suppresses the VEGF mRNA induction in MT clones without affecting the VEGF expression in control clones
hemopexin
-
soluble hemopexin domain inhibits collagenolysis by preventing dimerization
-
herbimycin-A
-
strongly inhibits up-regulation effect of VEGF-A by MT1-MMP
MT1-MMP siRNA
-
collagen degrading activity is completely lost when MT1-MMP expressing cells are transfected with 100 nM MT1-MMP siRNA
-
N,N'-bis(4-[[(3R)-3-[(biphenyl-4-ylsulfonyl)amino]-4-(hydroxyamino)-4-oxobutyl]amino]-4-oxobutyl)benzene-1,3-dicarboxamide
-
N,N'-bis[(3R)-3-[(biphenyl-4-ylsulfonyl)amino]-4-(hydroxyamino)-4-oxobutyl]benzene-1,3-dicarboxamide
-
N,N'-bis[4-[(2-[[(2R)-4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-1-(hydroxyamino)-1-oxobutan-2-yl][(4'-methoxybiphenyl-4-yl)sulfonyl]amino]ethyl)amino]-4-oxobutyl]benzene-1,3-dicarboxamide
-
N-(2-[[(2R)-4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-1-(hydroxyamino)-1-oxobutan-2-yl][(4'-methoxybiphenyl-4-yl)sulfonyl]amino]ethyl)-N'-(2-[[4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-1-(hydroxyamino)-1-oxobutan-2-yl][(4'-methoxybiphenyl-4-yl)sulfonyl]
modelling ofcompound 6 binding to dimeric MT1-MMP (catalytic domains)
N-hydroxy-4-([4-[4-(2-hydroxyphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-([4-[4-(2-methoxyphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-([4-[4-(2-methylphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-([4-[4-(3-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-([4-[4-(4-methoxy-2-methylphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-([4-[4-(4-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-([4-[4-(4-methylphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-[[4-(4-phenylpiperazin-1-yl)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-[[4-(4-phenylpiperidin-1-yl)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
-
N4-hydroxyamino-2-isobutyl-3-(thienylthiomethyl) succinyl]-L-phenylalamine-methylamide
-
-
PD98059
-
inhibits MMP-2 processing in HT1080 cells
Rac1
-
inhibits both enzyme activity and dimerization
-
Rac1(N17Rac)
-
coexpression wit MT1-MMP cDNAs leads to complete inhibition of migration
-
RECK
membrane anchor type proteinase inhibitor
-
reversion-inducing cysteine rich protein
-
-
-
reversion-inducing-cysteine-rich protein
-
-
-
RO28-2653
-
reduces the VEGF mRNA levels in MT clones but does not affect the basal VEGF mRNA levels in control clones
TAPI-1
-
inhibits the shedding of the MT1-MMP 18 kDa form
TIMP-1
-
TIMP-1 from brain is upregulated in in the infarcted tissue compared to healthy control areas, overview
-
TIMP-1 mutant forms
-
TIMP-1(T98L), TIMP-1(V4A), TIMP-1(P6V), TIMP-1(V4S), TIMP-1(P6S), TIMP-1(M66I), TIMP-1(P6A), TIMP-1(M66V), TIMP-1(M66A), TIMP-1(T2S), TIMP-1(M66L), TIMP-1(M66G), TIMP-1(V69L), TIMP-1(M66K), TIMP-1(V4A/P6V/T98L). TIMP-1 is inactive against MT1-MMP. TIMP-1 can be transformed into an active inhibitor against MT1-MMP by the mutation T98L. The resultant mutant displays inhibitory characteristics of a slow, tight binding inhibitor. The potency of the mutant can be further enhanced by the introduction of the mutations V4A and P6V
-
tissue inhibitor of matrix metalloproteinase-1
-
i.e. TIMP-1, recombinant, human
-
tissue inhibitor of matrix metalloproteinases-1
-
weak inhibitor
-
tissue inhibitor of matrix metalloproteinases-2
-
effective inhibitor
-
tissue inhibitor of matrix metalloproteinases-3
-
effective inhibitor
-
tissue inhibitor of metalloproteinase 2
-
-
Tissue inhibitor of metalloproteinase-1
-
TIMP-1
-
Tissue inhibitor of metalloproteinase-2
-
-
-
tissue inhibitor of metalloproteinases-2
-
tissue inhibitor of MMP-2
-
tissue inhibitor of MMP-3
-
i.e. TIMP-3
-
tissue inhibitor of MMP-4
-
i.e. TIMP-4
-
BB94

-
inhibits endothelial cell invasion
BB94
0.01 mM, dose dependent
BB94
-
supresses migration of HT1080 cells on type I collagen to 69%
BB94
-
reduces the VEGF mRNA levels in MT clones but does not affect the basal VEGF mRNA levels in control clones
BB94
-
maturation of MT1-MMP normally occurs
DX-2400

-
represents a highly selective fully MMP-14 inhibitory antibody discovered using phage display technology. DX-2400 blocks proMMP-2 processing on tumor and endothelial cells, inhibits angiogenesis and slows tumor progression and formation of metastatic lesions in xenograft models
-
DX-2400
-
represents a highly selective fully MMP-14 inhibitory antibody discovered using phage display technology. DX-2400 blocks proMMP-2 processing on tumor and endothelial cells, inhibits angiogenesis and slows tumor progression and formation of metastatic lesions in xenograft models
-
DX-2400
-
represents a highly selective fully MMP-14 inhibitory antibody discovered using phage display technology. DX-2400 blocks proMMP-2 processing on tumor and endothelial cells, inhibits angiogenesis and slows tumor progression and formation of metastatic lesions in xenograft models
-
DX-2400
enzyme activity is inhibited with 65.8 nM or 658 nM of the enzyme function-blocking antibody DX-2400
-
DX-2400
-
represents a highly selective fully MMP-14 inhibitory antibody discovered using phage display technology. DX-2400 blocks proMMP-2 processing on tumor and endothelial cells, inhibits angiogenesis and slows tumor progression and formation of metastatic lesions in xenograft models
-
furin

concanavalin A-induced pro-matrix metalloproteinase 2 activation is inhibited in human uterine cervical fibroblasts, but not in rabbit dermal fibroblasts
-
furin
-
inhibits MT1-MMP partitioning at the plasma membrane
-
furin
-
concanavalin A-induced pro-matrix metalloproteinase 2 activation is inhibited in human uterine cervical fibroblasts, but not in rabbit dermal fibroblasts
-
GM6001

hydroxamate inhibitor, 0.001 mM, converts protease into a cell surface receptor for receptor of complement component 1q and promotes co-precipitation of the enzyme with the soluble receptor protein
GM6001
-
fully blocks proteolysis of PA83 by MT1-MMP, inhibits MT1-MMP-dependent activation of proMMP-2
GM6001
-
blocks MT1-MMP autolytic processing
GM6001
blocks conversion of active 50 kDa wild type MT1-MMP to a 37 kDa species, inhibits autolysis of both wild type and CHO-4 MT1-MMP in a dose-dependent manner and with a similar inhibitory profile
GM6001
-
pan-metalloprotease inhibitor inhibits degradation of apolipoprotein E
GM6001
-
a broad-spectrum metalloproteinase inhibitor
GM6001
-
broad-spectrum matrix metalloproteinase inhibitor, strong inhibition
GM6001
-
a broad-spectrum metalloproteinase inhibitor
ilomastat

inhibits processing to the mature form of the enzyme
marimastat

inhibits production of 18 kDa fragment during autocatalytic processing
marimastat
-
strong inhibition
testican 3

including its variant N-Tes
-
TIMP-2

-
inhibits endothelial cell invasion
-
TIMP-2
tissue inhibitor of metalloproteinases
-
TIMP-2
inhibits production of 18 kDa fragment during autocatalytic processing
-
TIMP-2
rapid binding to catalytic site of enzyme
-
TIMP-2
-
specificity of inhibitor binding of MT1-MMP, shedding of MT1-MMP ectodomain alters the balance of TIMP-2 between the cell surface and the pericellular space
-
TIMP-2
-
supresses migration of HT1080 cells on type I collagen to 62%
-
TIMP-2
-
blocks up-regulation of VEGF-A by MT1-MMP
-
TIMP-2
-
totally abolishes substrate degradation
-
TIMP-2
-
inhibitory interaction with the catalytically competent MT1-MMP active site, prevents autolytic processing
-
TIMP-2
under in vivo conditions primary inhibitor of MT1-MMP, increases endocytosis of wild type MT1-MMP
-
TIMP-2
-
potent inhibitor
-
TIMP-2
-
inhibits degradation of apolipoprotein E
-
TIMP-2
-
highly produced in brain microvessels
-
TIMP-2
-
natural inhibitor of MT1-MMP
-
TIMP-2
-
0.0002 mM, dose dependent
-
TIMP-3

-
inhibits endothelial cell invasion
-
TIMP-3
tissue inhibitor of metalloproteinases
-
TIMP-3
rapid binding to catalytic site of enzyme
-
TIMP-3
-
potent inhibitor
-
TIMP-3
-
during ischemia, loss of inhibitory control leading to increased MT1-MMP activity
-
TIMP-4

tissue inhibitor of metalloproteinases
-
TIMP-4
inhibits production of 18 kDa fragment during autocatalytic processing
-
TIMP-4
-
during ischemia, loss of inhibitory control leading to increased MT1-MMP activity
-
tissue inhibitor of metalloproteinases-2

-
-
-
tissue inhibitor of metalloproteinases-2
-
-
tissue inhibitor of MMP-2

-
MMP-2 activation involves tissue inhibitor of MMP-2, i.e. TIMP-2, as a bridging molecule between MT1-MMP and pro-MMP-2. Thus, net activity of MT1-MMP and MMP-2 is regulated in a complex manner depending on TIMP-2 concentration. MT1-MMP auto-degradation is suppressed in the presence of TIMP-2, and MT1-MMP/TIMP-2 complex accumulates on cell surface. MT1-MMP cannot cleave other direct substrates at the TIMP-2 level that induces efficient pro-MMP-2 processing
-
tissue inhibitor of MMP-2
-
MMP-2 activation involves tissue inhibitor of MMP-2, i.e. TIMP-2, as a bridging molecule between MT1-MMP and pro-MMP-2. Thus, net activity of MT1-MMP and MMP-2 is regulated in a complex manner depending on TIMP-2 concentration. MT1-MMP auto-degradation is suppressed in the presence of TIMP-2, and MT1-MMP/TIMP-2 complex accumulates on cell surface. MT1-MMP cannot cleave other direct substrates at the TIMP-2 level that induces efficient pro-MMP-2 processing
-
additional information

-
TIMP-1 does not inhibit endothelial cell invasion
-
additional information
no inhibitor: TIMP-1
-
additional information
no inhibitor: TIMP-1
-
additional information
-
no inhibitor: TIMP-1
-
additional information
no inhibitor: TIMP-1
-
additional information
-
mercaptosulfide and hydroxamate inhibitors
-
additional information
-
mercaptosulfide inhibitors, interacting exclusively at the enzyme active site, strong stereoselectivity at the P1' and zinc-binding groups, competitive and reverse inhibition
-
additional information
-
migration of HT1080 cells on type I collagen not supressed by TIMP-1
-
additional information
-
TIMP-1 does not block up-regulation of VEGF-A by MT1-MMP, aprotinin, Pefabloc SC, leupeptin and pepstatin A fail to modulate the VEGF expression, wortmannin, PD98059 nor SB203580 affect MT1-MMP-mediated VEGF induction
-
additional information
-
cells cotransfected with TIMP-1 cDNA along with MT1-MMP and pMMP-2 cDNAs result in partial inhibition of substrate degradation, down to the basal digestion level resulting from MT1-MMP alone, wortmannin and PD98059 do not interfer with MT1-MMP-induced cell migration, CDC42 (N17) and RhoA(N19) have no effect on MT1-MMP-dependent cell migration
-
additional information
-
not inhibited by tissue inhibitor of metalloproteinases-1
-
additional information
-
not inhibited by tissue inhibitor of metalloproteinase-1
-
additional information
-
not inhibited by TIMP-1
-
additional information
-
not inhibited by TIMP-1
-
additional information
-
not inhibited by TIMP-1
-
additional information
-
MT1-MMP is inhibited by endogenous inhibitors TIMP-2, -3, and -4, but not by TIMP-1. MT1-MMP on cell surface rapidly turns over by auto-degradation or clathrin-dependent internalization. MT1-MMP inactivated by TIMP-2 avoids auto-degradation, and accumulates on the cell surface, overview
-
additional information
-
not inhibited by E-64 and aprotinin
-
additional information
design, synthesis, and biological evaluation of bifunctional inhibitors of membrane type 1 matrix metalloproteinase (MT1-MMP), overview
-
additional information
-
insensitive to TIMP-1
-
additional information
-
MT1-MMP on cell surface rapidly turns over by auto-degradation or clathrin-dependent internalization. MT1-MMP inactivated by TIMP-2 avoids auto-degradation, and accumulates on the cell surface, overview
-
additional information
-
synthesis of a series of phenyl piperidine a-sulfone hydroxamate derivatives, inhibitory potencies on different MMPs, overview. No inhibition by derivatives 1-cyclopropyl-N-hydroxy-4-[[4-(4-phenylpiperazin-1-yl)phenyl]sulfonyl]piperidine-4-carboxamide, 4-([4-[4-(2,4-dimethylphenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide, N-hydroxy-4-[(4-[4-[3-(trifluoromethyl)phenyl]piperazin-1-yl]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide, N-hydroxy-4-([4-[4-(2-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide, N-hydroxy-4-([4-[4-(2-methylphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide, 4-([4-[4-(2-chlorophenyl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide, N-hydroxy-4-[(4-[4-[2-(trifluoromethyl)phenyl]piperidin-1-yl]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide, 4-([4-[4-(2-ethoxyphenyl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide, 4-([4-[4-(4'-fluorobiphenyl-4-yl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide, and 4-[(4-[4-[2-ethyl-5-(propan-2-yl)phenyl]piperidin-1-yl]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00344
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2
pH 7.5, 37ưC, mature and mutant enzyme
0.0151 - 0.0368
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
-
0.0003 - 0.32
collagen I alpha-1 chain
-
0.00065 - 0.12
collagen I alpha-2 chain
-
0.00086 - 0.17
collagen type I alpha-1 chain
-
0.00025 - 0.53
collagen type I alpha-2 chain
-
0.0006 - 0.0028
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
0.009 - 0.01
MOCAcPLGLA2pr-dinitrophenol-A-RNH2
0.000034
type I collagen chain alpha-1
-
at 37ưC
-
0.000035
type I collagen chain alpha-2
-
at 37ưC
-
additional information
additional information
-
0.0151
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2

pH not specified in the publication, 37ưC, recombinant wild-type membrane-bound enzyme
-
0.0186
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37ưC, recombinant soluble enzyme
-
0.0234
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37ưC, recombinant enzyme mutant lacking the C-terminal domain
-
0.0368
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37ưC, recombinant enzyme mutant lacking the HPX domain
-
0.0003
collagen I alpha-1 chain

-
pH not specified in the publication, 37ưC, MMP-1: 1-protonated
-
0.00077
collagen I alpha-1 chain
-
pH not specified in the publication, 37ưC, MMP-1: 2-protonated
-
0.0027
collagen I alpha-1 chain
-
pH not specified in the publication, 37ưC, MMP-1: 0-protonated
-
0.32
collagen I alpha-1 chain
-
pH not specified in the publication, 37ưC, MMP-1: 3-protonated
-
0.00065
collagen I alpha-2 chain

-
pH not specified in the publication, 37ưC, MMP-1: 3-protonated
-
0.0031
collagen I alpha-2 chain
-
pH not specified in the publication, 37ưC, MMP-1: 0-protonated
-
0.0079
collagen I alpha-2 chain
-
pH not specified in the publication, 37ưC, MMP-1: 1-protonated
-
0.12
collagen I alpha-2 chain
-
pH not specified in the publication, 37ưC, MMP-1: 2-protonated
-
0.00086
collagen type I alpha-1 chain

-
1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
0.045
collagen type I alpha-1 chain
-
0-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
0.12
collagen type I alpha-1 chain
-
3-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
0.17
collagen type I alpha-1 chain
-
2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
0.00025
collagen type I alpha-2 chain

-
1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
0.004
collagen type I alpha-2 chain
-
2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
0.14
collagen type I alpha-2 chain
-
3-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
0.53
collagen type I alpha-2 chain
-
0-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
0.0006
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2

pH 7.0, 10ưC, recombinant enzyme
0.0018
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 25ưC, recombinant enzyme
0.0021
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 30ưC, recombinant enzyme
0.0028
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 37ưC, recombinant enzyme
0.009
MOCAcPLGLA2pr-dinitrophenol-A-RNH2

pH 7.5, Tyr112-Gly284 fragment
0.01
MOCAcPLGLA2pr-dinitrophenol-A-RNH2
pH 7.5, Tyr112-Gly288 fragment
additional information
additional information

Michaelis-Menten kinetics
-
additional information
additional information
-
increase in substrate triple-helical thermal stability is not detrimental to enzyme binding of substrate
-
additional information
additional information
steady-state kinetics and thermodynamics over a wide range of temperatures and pressures, stopped-flow fluorescence technique
-
additional information
additional information
-
steady-state kinetics and thermodynamics over a wide range of temperatures and pressures, stopped-flow fluorescence technique
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.14 - 0.84
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
-
0.019 - 1.1
collagen I alpha-1 chain
-
1.52 - 255.6
collagen I alpha-2 chain
-
0.3 - 10.41
collagen type I alpha-1 chain
-
0.0089 - 58.61
collagen type I alpha-2 chain
-
0.33 - 6.8
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
0.02 - 0.055
MOCAcPLGLA2pr-dinitrophenol-A-RNH2
1.05
type I collagen chain alpha-1
-
at 37ưC
-
0.99
type I collagen chain alpha-2
-
at 37ưC
-
additional information
additional information
-
increase in substrate triple-helical thermal stability is detrimental to enzyme turnover of substrate
-
0.14
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2

pH not specified in the publication, 37ưC, recombinant wild-type membrane-bound enzyme
-
0.2
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37ưC, recombinant enzyme mutant lacking the HPX domain
-
0.21
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37ưC, recombinant enzyme mutant lacking the C-terminal domain
-
0.84
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37ưC, recombinant soluble enzyme
-
0.019
collagen I alpha-1 chain

-
pH not specified in the publication, 37ưC, MMP-1: 1-protonated
-
0.47
collagen I alpha-1 chain
-
pH not specified in the publication, 37ưC, MMP-1: 0-protonated
-
0.68
collagen I alpha-1 chain
-
pH not specified in the publication, 37ưC, MMP-1: 2-protonated
-
1.1
collagen I alpha-1 chain
-
pH not specified in the publication, 37ưC, MMP-1: 3-protonated
-
1.52
collagen I alpha-2 chain

-
pH not specified in the publication, 37ưC, MMP-1: 3-protonated
-
5.79
collagen I alpha-2 chain
-
pH not specified in the publication, 37ưC, MMP-1: 1-protonated
-
9.89
collagen I alpha-2 chain
-
pH not specified in the publication, 37ưC, MMP-1: 0-protonated
-
255.6
collagen I alpha-2 chain
-
pH not specified in the publication, 37ưC, MMP-1: 2-protonated
-
0.3
collagen type I alpha-1 chain

-
1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
0.43
collagen type I alpha-1 chain
-
2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
4.56
collagen type I alpha-1 chain
-
0-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
10.41
collagen type I alpha-1 chain
-
4-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
0.0089
collagen type I alpha-2 chain

-
1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
0.014
collagen type I alpha-2 chain
-
2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
4.09
collagen type I alpha-2 chain
-
4-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
58.61
collagen type I alpha-2 chain
-
0-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
0.33
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2

pH 7.0, 10ưC, recombinant enzyme
2.1
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 25ưC, recombinant enzyme
3.4
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 30ưC, recombinant enzyme
6.8
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 37ưC, recombinant enzyme
0.02
MOCAcPLGLA2pr-dinitrophenol-A-RNH2

pH 7.5, Tyr112-Gly288 fragment
0.055
MOCAcPLGLA2pr-dinitrophenol-A-RNH2
pH 7.5, Tyr112-Gly284 fragment
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5.44 - 45.2
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
-
3.4 - 880
collagen I alpha-1 chain
-
730 - 3200
collagen I alpha-2 chain
-
2.5 - 360
collagen type I alpha-1 chain
-
3.5 - 350
collagen type I alpha-2 chain
-
550 - 2429
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
5.44
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2

pH not specified in the publication, 37ưC, recombinant enzyme mutant lacking the HPX domain
-
8.97
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37ưC, recombinant enzyme mutant lacking the C-terminal domain
-
9.27
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37ưC, recombinant wild-type membrane-bound enzyme
-
45.2
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
pH not specified in the publication, 37ưC, recombinant soluble enzyme
-
3.4
collagen I alpha-1 chain

-
pH not specified in the publication, 37ưC, MMP-1: 3-protonated
-
63
collagen I alpha-1 chain
-
pH not specified in the publication, 37ưC, MMP-1: 1-protonated
-
170
collagen I alpha-1 chain
-
pH not specified in the publication, 37ưC, MMP-1: 0-protonated
-
880
collagen I alpha-1 chain
-
pH not specified in the publication, 37ưC, MMP-1: 2-protonated
-
730
collagen I alpha-2 chain

-
pH not specified in the publication, 37ưC, MMP-1: 1-protonated
-
2100
collagen I alpha-2 chain
-
pH not specified in the publication, 37ưC, MMP-1: 2-protonated
-
2300
collagen I alpha-2 chain
-
pH not specified in the publication, 37ưC, MMP-1: 3-protonated
-
3200
collagen I alpha-2 chain
-
pH not specified in the publication, 37ưC, MMP-1: 0-protonated
-
2.5
collagen type I alpha-1 chain

-
2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
88
collagen type I alpha-1 chain
-
4-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
100
collagen type I alpha-1 chain
-
O-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
360
collagen type I alpha-1 chain
-
1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
3.5
collagen type I alpha-2 chain

-
2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
30
collagen type I alpha-2 chain
-
4-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
110
collagen type I alpha-2 chain
-
O-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
350
collagen type I alpha-2 chain
-
1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37ưC
-
550
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2

pH 7.0, 10ưC, recombinant enzyme
1167
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 25ưC, recombinant enzyme
1619
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 30ưC, recombinant enzyme
2429
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
pH 7.0, 37ưC, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0000039
(2R)-4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-N-hydroxy-2-[[(4'-methoxybiphenyl-4-yl)sulfonyl](propan-2-yloxy)amino]butanamide
Homo sapiens
pH 7.5, 37ưC
0.000034
(2R)-4-(acetylamino)-2-[(biphenyl-4-ylsulfonyl)amino]-N-hydroxybutanamide
Homo sapiens
pH 7.5, 37ưC
0.01
1-cyclopropyl-N-hydroxy-4-[(4-[4-[4-(trifluoromethyl)phenyl]piperazin-1-yl]phenyl)sulfonyl]piperidine-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
4-([4-[4-(2-chlorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
4-([4-[4-(2-fluorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
4-([4-[4-(4-chlorophenyl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.000023
CGS-27023A
Homo sapiens
pH 7.5, 37ưC
0.000041
N,N'-bis(4-[[(3R)-3-[(biphenyl-4-ylsulfonyl)amino]-4-(hydroxyamino)-4-oxobutyl]amino]-4-oxobutyl)benzene-1,3-dicarboxamide
Homo sapiens
pH 7.5, 37ưC
0.00008
N,N'-bis[(3R)-3-[(biphenyl-4-ylsulfonyl)amino]-4-(hydroxyamino)-4-oxobutyl]benzene-1,3-dicarboxamide
Homo sapiens
pH 7.5, 37ưC
0.000007
N,N'-bis[4-[(2-[[(2R)-4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-1-(hydroxyamino)-1-oxobutan-2-yl][(4'-methoxybiphenyl-4-yl)sulfonyl]amino]ethyl)amino]-4-oxobutyl]benzene-1,3-dicarboxamide
Homo sapiens
pH 7.5, 37ưC
0.000014
N-(2-[[(2R)-4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-1-(hydroxyamino)-1-oxobutan-2-yl][(4'-methoxybiphenyl-4-yl)sulfonyl]amino]ethyl)-N'-(2-[[4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-1-(hydroxyamino)-1-oxobutan-2-yl][(4'-methoxybiphenyl-4-yl)sulfonyl]
Homo sapiens
pH 7.5, 37ưC
0.01
N-hydroxy-4-([4-[4-(2-hydroxyphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
N-hydroxy-4-([4-[4-(2-methoxyphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
N-hydroxy-4-([4-[4-(2-methylphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.00286
N-hydroxy-4-([4-[4-(3-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
N-hydroxy-4-([4-[4-(4-methoxy-2-methylphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
N-hydroxy-4-([4-[4-(4-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.00822
N-hydroxy-4-([4-[4-(4-methylphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
N-hydroxy-4-[[4-(4-phenylpiperazin-1-yl)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
N-hydroxy-4-[[4-(4-phenylpiperidin-1-yl)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.