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2,4-dinitrophenyl-Arg-Pro-Leu-Ala-Ala-Trp-Arg-Ser-NH2 + H2O
?
-
-
-
?
2,4-dinitrophenyl-Arg-Pro-Leu-Ala-Arg-Trp-Arg-Ser-NH2 + H2O
?
-
-
-
?
2,4-dinitrophenyl-Arg-Pro-Leu-Ala-Glu-Trp-Arg-Ser-NH2 + H2O
?
-
-
-
?
2,4-dinitrophenyl-Arg-Pro-Leu-Ala-Leu-Trp-Arg-Ser-NH2 + H2O
?
-
-
-
?
2,4-dinitrophenyl-Arg-Pro-Leu-Ala-Lys-Trp-Arg-Ser-NH2 + H2O
?
-
-
-
?
2,4-dinitrophenyl-Arg-Pro-Leu-Ala-Phe-Trp-Arg-Ser-NH2 + H2O
?
-
-
-
?
2,4-dinitrophenyl-Arg-Pro-Leu-Ala-Ser-Trp-Arg-Ser-NH2 + H2O
?
-
-
-
?
2,4-dinitrophenyl-Arg-Pro-Leu-Ala-Trp-Trp-Arg-Ser-NH2 + H2O
?
-
-
-
?
2,4-dinitrophenyl-Arg-Pro-Leu-Ala-Tyr-Trp-Arg-Ser-NH2 + H2O
?
-
-
-
?
2-aminobenzoyl-ASVATELRAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-ASVATE + LRAQ-2-(2,4-dinitrophenyl)aminoethylamide
2-aminobenzoyl-EAAPSSVIAATE-2-(2,4-dinitrophenyl)aminoethylamide + H2O
?
2-aminobenzoyl-EPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-EPLA + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
2-aminobenzoyl-GAMFLEAIPMSIP-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-GAMF + LEAIPMSIP-2-(2,4-dinitrophenyl)aminoethylamide
2-aminobenzoyl-GPLELEEAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-GPLE + LEEAQ-2-(2,4-dinitrophenyl)aminoethylamide
2-aminobenzoyl-GPLGLERAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-GPLG + LERAQ-2-(2,4-dinitrophenyl)aminoethylamide
2-aminobenzoyl-GPLGLREAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-GPLG + LREAQ-2-(2,4-dinitrophenyl)aminoethylamide
2-aminobenzoyl-PLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-PLA + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
2-aminobenzoyl-PLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-PLG + LEEA-2-(2,4-dinitrophenyl)aminoethylamide
2-aminobenzoyl-RGLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RGLA + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
2-aminobenzoyl-RNALAVERTAS-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RNALA + VERTAS-2-(2,4-dinitrophenyl)aminoethylamide
2-aminobenzoyl-RPLALEESQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LEESQ-2-(2,4-dinitrophenyl)aminoethylamide
2-aminobenzoyl-RPLALRRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LRRSQ-2-(2,4-dinitrophenyl)aminoethylamide
2-aminobenzoyl-RPLALWEEQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LWEEQ-2-(2,4-dinitrophenyl)aminoethylamide
2-aminobenzoyl-RPLALWESQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LWESQ-2-(2,4-dinitrophenyl)aminoethylamide
2-aminobenzoyl-RPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
2-aminobenzoyl-RPLELWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLE + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
2-aminobenzoyl-RPLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLG + LEEA-2-(2,4-dinitrophenyl)aminoethylamide
2-aminobenzoyl-RPLGLGAAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLG + LGAAQ-2-(2,4-dinitrophenyl)aminoethylamide
2-aminobenzoyl-RPLGLGGAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLG + LGGAQ-2-(2,4-dinitrophenyl)aminoethylamide
2-aminobenzoyl-RPLGLWGAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLG + LWGAQ-2-(2,4-dinitrophenyl)aminoethylamide
alpha-1-antitrypsin + H2O
?
-
recombinant enzyme rHME
-
?
alpha-casein + H2O
?
-
-
-
-
?
alpha1-antitrypsin + H2O
?
beta-casein + H2O
?
-
-
-
-
?
chondroitan sulfate + H2O
?
-
recombinant enzyme rHME
-
?
Collagen type I + H2O
?
-
the potential of MMP-12 in recognizing sites in human skin collagen types I and III has been investigated. The catalytic domain of MMP-12 binds to the triple helix and cleaves the typical sites -Gly775-Leu776- in alpha-2 type I collagen and -Gly775-Ile776- in alpha-1 type I and type III collagens and at multiple other sites in both collagen types. The region around these typical sites contains comparatively less prolines, of which some have been proven to be only partially hydroxylated
-
-
?
Collagen type III + H2O
?
-
the potential of MMP-12 in recognizing sites in human skin collagen types I and III has been investigated. The catalytic domain of MMP-12 binds to the triple helix and cleaves the typical sites -Gly775-Leu776- in alpha-2 type I collagen and -Gly775-Ile776- in alpha-1 type I and type III collagens and at multiple other sites in both collagen types. The region around these typical sites contains comparatively less prolines, of which some have been proven to be only partially hydroxylated
-
-
?
DQ-collagen I + H2O
?
-
-
-
-
?
DQ-collagen IV + H2O
?
-
-
-
-
?
elastin fELN-125 + H2O
?
-
-
-
-
?
enactin + H2O
?
-
recombinant enzyme rHME
-
?
extracellular matrix protein + H2O
?
-
may be required for macrophages to penetrate basement membranes and remodel injured tissue during inflammation
-
?
fEln-100 + H2O
?
-
alpha-elastin
-
-
?
heparan sulfate + H2O
?
-
recombinant enzyme rHME
-
?
human apolipoprotein (alpha) + H2O
?
-
cleaves in the linker region between kringles IV-4 and IV-5
-
?
Insulin B-chain + H2O
?
-
hydrolyzes Ala-Leu and Tyr-Leu, not His10-Leu11, on amino side of Leu-residue, not Val-residue
-
-
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
Mca-Pro-Leu-Gly + Leu-Dpa-Ala-Arg-NH2
-
-
-
-
?
Mca-Pro-Leu-Gly-Leu-Glu-Glu-Ala-Dpa-NH2 + H2O
Mca-Pro-Leu-Gly + Leu-Glu-Glu-Ala-Dpa-NH2
-
selective cleavage, the Glu-Glu motif interacts with the S'2 and S'3 subsites of MMP-12
-
-
?
triple helical peptide alpha1(V) + H2O
?
-
collagen V fibrils
-
-
?
type-IV collagen + H2O
?
-
degradation
-
-
?
Elastin + H2O
additional information
-
2-aminobenzoyl-ASVATELRAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-ASVATE + LRAQ-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-ASVATELRAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-ASVATE + LRAQ-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-EAAPSSVIAATE-2-(2,4-dinitrophenyl)aminoethylamide + H2O
?
-
-
-
?
2-aminobenzoyl-EAAPSSVIAATE-2-(2,4-dinitrophenyl)aminoethylamide + H2O
?
-
-
-
?
2-aminobenzoyl-EPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-EPLA + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
minor cleavage site is E-/-PLA
-
-
?
2-aminobenzoyl-EPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-EPLA + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
minor cleavage site is E-/-PLA
-
-
?
2-aminobenzoyl-GAMFLEAIPMSIP-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-GAMF + LEAIPMSIP-2-(2,4-dinitrophenyl)aminoethylamide
minor cleavage sites are LEAI-/-P-/-MSIP
-
-
?
2-aminobenzoyl-GAMFLEAIPMSIP-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-GAMF + LEAIPMSIP-2-(2,4-dinitrophenyl)aminoethylamide
minor cleavage sites are LEAI-/-P-/-MSIP
-
-
?
2-aminobenzoyl-GPLELEEAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-GPLE + LEEAQ-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-GPLELEEAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-GPLE + LEEAQ-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-GPLGLERAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-GPLG + LERAQ-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-GPLGLERAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-GPLG + LERAQ-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-GPLGLREAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-GPLG + LREAQ-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-GPLGLREAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-GPLG + LREAQ-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-PLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-PLA + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
minor cleavage site is PL-/-A
-
-
?
2-aminobenzoyl-PLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-PLA + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
minor cleavage site is PL-/-A
-
-
?
2-aminobenzoyl-PLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-PLG + LEEA-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-PLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-PLG + LEEA-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-RGLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RGLA + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
minor cleavage site is LW-/-RSQ
-
-
?
2-aminobenzoyl-RGLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RGLA + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
minor cleavage site is LW-/-RSQ
-
-
?
2-aminobenzoyl-RNALAVERTAS-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RNALA + VERTAS-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-RNALAVERTAS-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RNALA + VERTAS-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-RPLALEESQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LEESQ-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-RPLALEESQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LEESQ-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-RPLALRRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LRRSQ-2-(2,4-dinitrophenyl)aminoethylamide
minor cleavage site is RPL-/-A
-
-
?
2-aminobenzoyl-RPLALRRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LRRSQ-2-(2,4-dinitrophenyl)aminoethylamide
minor cleavage site is RPL-/-A
-
-
?
2-aminobenzoyl-RPLALWEEQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LWEEQ-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-RPLALWEEQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LWEEQ-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-RPLALWESQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LWESQ-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-RPLALWESQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LWESQ-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-RPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
minor cleavage site is RPL-/-A
-
-
?
2-aminobenzoyl-RPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
minor cleavage site is RPL-/-A
-
-
?
2-aminobenzoyl-RPLELWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLE + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
minor cleavage site is RPL-/-E
-
-
?
2-aminobenzoyl-RPLELWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLE + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
minor cleavage site is RPL-/-E
-
-
?
2-aminobenzoyl-RPLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLG + LEEA-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-RPLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLG + LEEA-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-RPLGLGAAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLG + LGAAQ-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-RPLGLGAAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLG + LGAAQ-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-RPLGLGGAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLG + LGGAQ-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-RPLGLGGAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLG + LGGAQ-2-(2,4-dinitrophenyl)aminoethylamide
-
-
-
?
2-aminobenzoyl-RPLGLWGAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLG + LWGAQ-2-(2,4-dinitrophenyl)aminoethylamide
minor cleavage site is RPL-/-G
-
-
?
2-aminobenzoyl-RPLGLWGAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLG + LWGAQ-2-(2,4-dinitrophenyl)aminoethylamide
minor cleavage site is RPL-/-G
-
-
?
alpha1-antitrypsin + H2O
?
-
-
-
-
?
alpha1-antitrypsin + H2O
?
-
-
-
-
?
casein + H2O
?
-
-
-
-
?
casein + H2O
?
-
degradation
-
-
?
Elastin + H2O
?
-
-
-
?
Elastin + H2O
?
-
-
-
-
?
Elastin + H2O
?
-
MMP-12 is active against multiple extracellular protein substrates such as elastin, its effect on elastin is central to emphysema in the lung and photoaging of skin, its expression in the skin increases on photodamaged skin and upon aging
-
-
?
Elastin + H2O
?
-
cleavage site determination and peptide mapping by mass spectrometry, based on the human tropoelastin isoform 9 sequence, SwissProt accession number P15502-9, preference of amino acids Ala and Gly at subsites, overview
-
-
?
Elastin + H2O
?
-
a key structural component of the lung extracellular matrix
-
-
?
Elastin + H2O
?
-
-
-
-
?
Elastin + H2O
?
-
degradation
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
recombinant enzyme rHME
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
degradation
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
recombinant enzyme rHME
-
?
Laminin + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
degradation
-
-
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
-
soluble Knight's peptide substrate MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
-
?
TNF-alpha + H2O
?
-
-
-
-
?
TNF-alpha + H2O
?
-
-
-
-
?
Type IV collagen + H2O
?
-
-
-
-
?
Type IV collagen + H2O
?
-
recombinant enzyme rHME
-
?
Type IV collagen + H2O
?
-
-
-
-
?
Elastin + H2O
additional information
-
-
-
-
-
?
Elastin + H2O
additional information
-
-
preferentially cleaves on amino-side of Leus, not Val
products of elastin hydrolysis are predominantly high MW peptides, MW 90000-100000
?
Elastin + H2O
additional information
-
-
bovine ligament elastin
-
-
?
additional information
?
-
able to degrade all components of extracellular matrix
-
?
additional information
?
-
-
able to degrade all components of extracellular matrix
-
?
additional information
?
-
-
important role in inflammatory processes contributing to tissue remodelling
-
?
additional information
?
-
-
macrophage-derived overexpression of MMP-12 causes accelerated atherosclerosis. Overexpression of human MMP-12 in macrophages of rabbits results in enhanced atherosclerosis
-
-
?
additional information
?
-
-
MMP-12 exacerbates atherosclerosis, emphysema, aortic aneurysm, rheumatoid arthritis, and inflammatory bowel disease
-
-
?
additional information
?
-
-
the enzyme induces inflammation in murine airways after direct instillation eliciting the inflammatory response by neutrophil influx, cytokine release, and gelatinase activation, and delayed response by macrophage recruitment, overview
-
-
?
additional information
?
-
-
the enzyme induces inflammation in murine airways after direct instillation eliciting the inflammatory response by neutrophil influx, cytokine release, and gelatinase activation, and delayed response by macrophage recruitment, resident alveolar macrophages and recruited neutrophils do not play a role in the delayed macrophage recruitment induced by MMP-12, overview
-
-
?
additional information
?
-
-
the enzyme plays an important role in inflammatory processes and is involved in a number of physiological or pathological situations, such as conversion of plasminogen into angiostatin, allergic airway inflammation, vascular remodeling or alteration, as well as emphysema
-
-
?
additional information
?
-
-
active site structure, surfaces and internal pocket between helix B and beta-strand IV in the active-site cleft, overview
-
-
?
additional information
?
-
-
HME has the ability to convert plasminogen into angiostatin, an essential and potent inhibitor of endothelial cell proliferation and tumor angiogenesis
-
-
?
additional information
?
-
-
MMP-12 has in vitro, a wide variety of potential substrates, including type IV collagen, fibronectin, laminin, and gelatin, as well as non-matrix proteins such as alpha1-antitrypsin and latent TNF-alpha
-
-
?
additional information
?
-
the catalytic domain of MMP-12 is unique among MMPs in that it is very highly active on numerous substrates including elastin
-
-
?
additional information
?
-
-
the catalytic domain of MMP-12 is unique among MMPs in that it is very highly active on numerous substrates including elastin
-
-
?
additional information
?
-
substrate specificity analysis using several peptide substrates, peptide design and evaluation, docking study, detailed overview
-
-
?
additional information
?
-
-
substrate specificity analysis using several peptide substrates, peptide design and evaluation, docking study, detailed overview
-
-
?
additional information
?
-
-
acetyl-Ala-Ala-Ala 4-nitroanilide or benzyloxycarbonyl-Ala 2-naphthyl esters
-
-
?
additional information
?
-
-
no substrates are Glu-Ala-Leu-Tyr-Leu-Val (i.e. residues 13-18 of insulin B-chain)
-
-
?
additional information
?
-
-
MMP-12 does not appear to be involved in the fibrogenic pathway of bleomycin-induced lung injury. MMP-12 deficiency does not influence the bleomycin-induced raise of neither TGF-beta-1 nor TIMP-1 in lung, which are described as important pro-fibrogenic effectors
-
-
?
additional information
?
-
-
protease-activated receptor 1, PAR-1, controls MMP-12 release
-
-
?
additional information
?
-
-
the enzyme is important for allowing macrophage migration through extracellular matrix, and probably plays an important role in the causation of inflammatory bowel disease, IBD, MMP-12 expression is increased in ulcerative colitis and in Crohns disease
-
-
?
additional information
?
-
-
no activity with interstitial collagens or gelatin
-
-
?
additional information
?
-
-
MMP12 has a direct bactericidal activity but is unable to kill certain bacteria such as those that have the ability to escape the phagosome, which is exerted by the C-terminal domain, that also alone shows bacterial killing activity
-
-
?
additional information
?
-
-
MMP12 is involved in bacterial clearance. Intracellular stores of MMP12 are mobilized to macrophage phagolysosomes after the ingestion of bacterial pathogens. Once inside phagolysosomes, MMP12 adheres to bacterial cell walls where it disrupts cellular membranes resulting in bacterial death. The bacterial killing requires the SR20 sequence, 344-SRNQLFLFKDEKYWLINNLV-363, which alone is also active, but shorter four-amino-acid peptides, Ser-Gly-Arg-Gln, Lys-Asp-Asp-Lys and Lys-Asp-Glu-Lys, do not show antimicrobial activity, suggesting that the loop structure of the protein is required for bacterial killing
-
-
?
additional information
?
-
-
MMP-12 has in vitro, a wide variety of potential substrates, including type IV collagen, fibronectin, laminin, and gelatin, as well as non-matrix proteins such as alpha1-antitrypsin and latent TNF-alpha
-
-
?
additional information
?
-
-
MMP12, through the catalytic domain, can cleave a variety of substrates in addition to elastin such as type IV collagen, fibronectin, and gelatin in in vitro assays
-
-
?
additional information
?
-
the catalytic domain of MMP-12 is unique among MMPs in that it is very highly active on numerous substrates including elastin
-
-
?
additional information
?
-
-
the catalytic domain of MMP-12 is unique among MMPs in that it is very highly active on numerous substrates including elastin
-
-
?
additional information
?
-
substrate specificity analysis using several peptide substrates, peptide design and evaluation, docking study, detailed overview
-
-
?
additional information
?
-
-
substrate specificity analysis using several peptide substrates, peptide design and evaluation, docking study, detailed overview
-
-
?
additional information
?
-
-
protease-activated receptor 1, PAR-1, controls MMP-12 release
-
-
?
additional information
?
-
-
the enzyme is involved in the development of chronic obstructive pulmonary disease and airway inflammation and is associated with allergic bronchial asthma, phenotype, overview
-
-
?
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(1S,5S,7R)-3-aza-6,8-dioxa-bicyclo[3.2.1]octane-3,7-dicarboxylic acid 7-[(biphenyl-4-ylmethyl)-amide] 3-hydroxyamide
-
-
(1S,5S,7R)-3-biphenyl-4-ylmethyl-2-oxo-3-aza-6,8-dioxa-bicyclo[3.2.1]octane-7-carboxylic acid
-
-
(1S,5S,7R)-3-biphenyl-4-ylmethyl-2-oxo-3-aza-6,8-dioxa-bicyclo[3.2.1]octane-7-carboxylic acid hydroxyamide
-
-
(1S,5S,7R)-3-biphenyl-4-ylmethyl-3-aza-6,8-dioxabicyclo[3.2.1]octane-7-carboxylic acid
-
-
(1S,5S,7R)-3-biphenyl-4-ylmethyl-3-aza-6,8-dioxabicyclo[3.2.1]octane-7-carboxylic acid hydroxyamide
-
-
(3R)-3-([[4-(4'-acetylbiphenyl-4-yl)-5-fluorothiophen-2-yl]carbonyl]amino)-3-phenylpropanoic acid
-
-
(3R)-3-[([5-fluoro-4-[4-(pyridin-4-yl)phenyl]thiophen-2-yl]carbonyl)amino]-3-phenylpropanoic acid
-
-
(3R)-3-[([5-fluoro-4-[4-(trifluoromethoxy)phenyl]thiophen-2-yl]carbonyl)amino]-3-phenylpropanoic acid
-
-
CGS-27023A
-
a hydroxamate inhibitor
dexamethasone
-
in vivo inhibition of the human enzyme in mice leading to inhibited cytokine release and neutrophil influx, overview
EGTA
-
less effective than EDTA, Ca2+ at a 3:1 ratio of Ca2+/EDTA protects and reverses partially, Zn2+ at a 1:10 ratio of Zn2+/EGTA protects and reverses
marimastat
-
in vivo inhibition of the human enzyme in mice leading to inhibited macrophage recruitment, neutrophil influx, and cytokine release, overview
N-(3-[(4-bromophenyl)(hydroxy)phosphoryl]-2-[3-[4-(dimethylamino)phenyl]isoxazol-5-yl]propanoyl)-L-alpha-glutamyl-L-alpha-glutamine
-
-
N-isobutyl-N-[4-methoxyphenylsulfonyl] glycyl hydroxamic acid
-
-
N-[(1R)-3-amino-3-oxo-1-phenylpropyl]-5-fluoro-4-[4-(trifluoromethoxy)phenyl]thiophene-2-carboxamide
-
-
N-[(2S,4S)-1-(ethoxymethoxy)-5-(hydroxyamino)-4-methyl-5-oxo-2-pentanyl]-4-phenoxybenzamide
i.e. ONO-4817, an MMP inhibitor
N-[3-[(4-bromophenyl)(hydroxy)phosphoryl]-2-[3-(3'-chlorobiphenyl-4-yl)isoxazol-5-yl]propanoyl]-L-alpha-glutamyl-L-alpha-glutamine
-
-
organic solvents
-
enzyme form B, above 0.5% v/v
-
Rabbit antiserum against purified elastase form B
-
-
-
rolipram
-
in vivo inhibition of the human enzyme in mice leading to inhibited neutrophil influx, overview
TIMP-1
-
a major fibrogenic effector in lungs. Indeed, upon fibrogenic stimuli, large amounts of TIMP-1 in the remodeling tissue are believed to contribute to the creation of a non-degrading environment, leading to the alteration of protease-anti-protease balance, extracellular matrix accumulation, and tissue fibrosis. MMP-12 deficiency does not seem to be involved in TIMP-1 regulation
-
tissue inhibitor of metalloproteinase
-
trans-4-[([[4-(4'-acetylbiphenyl-4-yl)-5-fluorothiophen-2-yl]carbonyl]amino)methyl]cyclohexanecarboxylic acid
-
-
trans-4-[[([3-[4-(trifluoromethoxy)phenyl]-1,2-thiazol-5-yl]carbonyl)amino]methyl]cyclohexanecarboxylic acid
-
-
trans-4-[[([4-[4-(trifluoromethoxy)phenyl]thiophen-2-yl]carbonyl)amino]methyl]cyclohexanecarboxylic acid
-
-
trans-4-[[([5-fluoro-4-[4-(trifluoromethoxy)phenyl]thiophen-2-yl]carbonyl)amino]methyl]cyclohexanecarboxylic acid
-
-
trans-4-[[([5-[4-(trifluoromethoxy)phenyl]-1,2-thiazol-3-yl]carbonyl)amino]methyl]cyclohexanecarboxylic acid
-
-
Zn2+
-
at a 3fold molar excess of Zn2+ over chelating agent
alpha2-Macroglobulin
-
SDS abolishes inhibition
-
alpha2-Macroglobulin
-
SDS abolishes inhibition
-
EDTA
-
Zn2+ at a 1:10 ratio of Zn2+/EDTA protects and reverses, not Ca2+, no reversal by Co2+ or Mg2+
GM6001
-
tissue inhibitor of metalloproteinase
-
i.e. TIMP-1, recombinant enzyme
-
tissue inhibitor of metalloproteinase
-
i.e. TIMP-1, recombinant enzyme
-
additional information
-
inhibition of MMP-12 may be a potential modality for the treatment of rheumatoid arthritis
-
additional information
-
inhibitor design and synthesis based on a 3-aza-6,8-dioxa-bicyclo[3.2.1]octane scaffold, library construction and screening, determination of affinity for the catalytic domain of MMP-12 by NMR, overview
-
additional information
-
role of the P'3 position in inhibitor selectivity, overview, interaction of compound 1 with the catalytic domain of MMP12, molecular modeling, overview
-
additional information
-
diisopropylphosphorofluoridate, PCMB, NEM, mersalyl, soybean trypsin inhibitor, acetyltetraalanylchloromethane, phosphoramidon, glycoprotein tissue inhibitor, alpha1-proteinase inhibitor; no inhibition by PMSF (form B)
-
additional information
-
compound E-64, i.e. trans-epoxysuccinyl-L-leucyl-amido-(4-guanidino)butane; no inhibition by PMSF (form B)
-
additional information
-
alpha1-antitrypsin, hirudin, aprotinin, and pertussis toxin, the G-protein coupled receptor inhibitor, suppress TNF-alpha and MMP-12 production by cigarette smoke-stimulated macrophage, while the PAR-1 agonist TRAP increases the release of MMP-12 and TNF-alpha, overview, TNF-alpha release in alveolar macrophages is related to MMP-12 secretion, alpha1-antitrypsin does not inhibit the activation of the MMP-12 proenzyme
-
additional information
-
MMP inhibitors applied in animal models of emphysema are successful in reducing lung inflammation
-
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.
0.0202 - 0.0249
2-aminobenzoyl-PLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
0.0047 - 0.0091
2-aminobenzoyl-PLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
0.0075 - 0.029
2-aminobenzoyl-RPLALEESQ-2-(2,4-dinitrophenyl)aminoethylamide
0.0123 - 0.0146
2-aminobenzoyl-RPLALWEEQ-2-(2,4-dinitrophenyl)aminoethylamide
0.0068 - 0.0138
2-aminobenzoyl-RPLALWESQ-2-(2,4-dinitrophenyl)aminoethylamide
0.0144 - 0.0156
2-aminobenzoyl-RPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
0.0088 - 0.0093
2-aminobenzoyl-RPLELWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
0.0103 - 0.0197
2-aminobenzoyl-RPLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
0.001 - 0.00466
fEln-100
-
0.113 - 0.241
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
0.0202
2-aminobenzoyl-PLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
0.0249
2-aminobenzoyl-PLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
0.0047
2-aminobenzoyl-PLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
0.0091
2-aminobenzoyl-PLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
0.0075
2-aminobenzoyl-RPLALEESQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
0.029
2-aminobenzoyl-RPLALEESQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
0.0123
2-aminobenzoyl-RPLALWEEQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
0.0146
2-aminobenzoyl-RPLALWEEQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
0.0068
2-aminobenzoyl-RPLALWESQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
0.0138
2-aminobenzoyl-RPLALWESQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
0.0144
2-aminobenzoyl-RPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
0.0156
2-aminobenzoyl-RPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
0.0088
2-aminobenzoyl-RPLELWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
0.0093
2-aminobenzoyl-RPLELWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
0.0103
2-aminobenzoyl-RPLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
0.0197
2-aminobenzoyl-RPLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
0.001
fEln-100
-
pH 7.5, 25°C, wild-type
-
0.00109
fEln-100
-
pH 7.5, 25°C, mutant D124Q/A182G
-
0.00114
fEln-100
-
pH 7.5, 25°C, mutant A182G
-
0.00115
fEln-100
-
pH 7.5, 25°C, mutant M103F
-
0.00115
fEln-100
-
pH 7.5, 25°C, mutant R117S
-
0.00119
fEln-100
-
pH 7.5, 25°C, mutant D124Q/M156E/I180S
-
0.00127
fEln-100
-
pH 7.5, 25°C, mutant D124Q/I180S
-
0.0013
fEln-100
-
pH 7.5, 25°C, mutant I180S
-
0.00135
fEln-100
-
pH 7.5, 25°C, mutant D124Q/M156E/F185Y
-
0.00145
fEln-100
-
pH 7.5, 25°C, mutant D124Q/M156E/T205K
-
0.00171
fEln-100
-
pH 7.5, 25°C, mutant D124Q/M156E/A182G
-
0.00175
fEln-100
-
pH 7.5, 25°C, mutant D124Q
-
0.00239
fEln-100
-
pH 7.5, 25°C, mutant M156E
-
0.0034
fEln-100
-
pH 7.5, 25°C, mutant D124Q/M156E
-
0.00399
fEln-100
-
pH 7.5, 25°C, mutant M156E/I180S
-
0.00466
fEln-100
-
pH 7.5, 25°C, mutant M156E/A182G
-
0.113
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/M156E/T205K
0.113
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant R117S
0.118
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant M156E/A182G
0.119
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant M156E/I180S
0.124
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/M156E
0.125
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q
0.125
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant M156E
0.128
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant M103F
0.129
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, wild-type
0.13
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant A182G
0.135
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/M156E/F185Y
0.17
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant I180S
0.18
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/M156E/I180S
0.194
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/A182G
0.202
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/M156E/A182G
0.241
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/I180S
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.85 - 1.5
2-aminobenzoyl-PLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
0.29 - 0.55
2-aminobenzoyl-PLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
0.26 - 2.4
2-aminobenzoyl-RPLALEESQ-2-(2,4-dinitrophenyl)aminoethylamide
0.17 - 1.3
2-aminobenzoyl-RPLALWEEQ-2-(2,4-dinitrophenyl)aminoethylamide
0.11 - 2.8
2-aminobenzoyl-RPLALWESQ-2-(2,4-dinitrophenyl)aminoethylamide
0.033 - 5.5
2-aminobenzoyl-RPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
0.014 - 1.4
2-aminobenzoyl-RPLELWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
0.19 - 3.8
2-aminobenzoyl-RPLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
6.8 - 24.1
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
0.85
2-aminobenzoyl-PLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
1.5
2-aminobenzoyl-PLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
0.29
2-aminobenzoyl-PLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
0.55
2-aminobenzoyl-PLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
0.26
2-aminobenzoyl-RPLALEESQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
2.4
2-aminobenzoyl-RPLALEESQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
0.17
2-aminobenzoyl-RPLALWEEQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
1.3
2-aminobenzoyl-RPLALWEEQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
0.11
2-aminobenzoyl-RPLALWESQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
2.8
2-aminobenzoyl-RPLALWESQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
0.033
2-aminobenzoyl-RPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
5.5
2-aminobenzoyl-RPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
0.014
2-aminobenzoyl-RPLELWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
1.4
2-aminobenzoyl-RPLELWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
0.19
2-aminobenzoyl-RPLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
3.8
2-aminobenzoyl-RPLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
0.001
fEln-100
-
pH 7.5, 25°C, mutant D124Q/M156E/A182G
-
0.001
fEln-100
-
pH 7.5, 25°C, mutant D124Q/M156E/I180S
-
0.0018
fEln-100
-
pH 7.5, 25°C, mutant D124Q/A182G
-
0.0024
fEln-100
-
pH 7.5, 25°C, mutant D124Q/I180S
-
0.0037
fEln-100
-
pH 7.5, 25°C, mutant I180S
-
0.0048
fEln-100
-
pH 7.5, 25°C, mutant D124Q/M156E/F185Y
-
0.0052
fEln-100
-
pH 7.5, 25°C, mutant M156E/I180S
-
0.0057
fEln-100
-
pH 7.5, 25°C, mutant A182G
-
0.0065
fEln-100
-
pH 7.5, 25°C, mutant D124Q/M156E/T205K
-
0.0072
fEln-100
-
pH 7.5, 25°C, mutant R117S
-
0.0092
fEln-100
-
pH 7.5, 25°C, mutant M103F
-
0.01
fEln-100
-
pH 7.5, 25°C, wild-type
-
0.0117
fEln-100
-
pH 7.5, 25°C, mutant M156E
-
0.0124
fEln-100
-
pH 7.5, 25°C, mutant D124Q
-
0.0143
fEln-100
-
pH 7.5, 25°C, mutant D124Q/M156E
-
0.021
fEln-100
-
pH 7.5, 25°C, mutant M156E/A182G
-
6.8
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant M156E/I180S
8.4
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/M156E/A182G
9.7
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/M156E/I180S
10.6
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/A182G
13.7
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant R117S
15.6
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant A182G
16.2
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/I180S
16.7
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/M156E
16.9
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant M156E
17.1
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q
17.2
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant M156E/A182G
17.3
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, wild-type
18
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/M156E/F185Y
18
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/M156E/T205K
18.7
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant M103F
24.1
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant I180S
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 - 170
2-aminobenzoyl-ASVATELRAQ-2-(2,4-dinitrophenyl)aminoethylamide
2 - 50
2-aminobenzoyl-EAAPSSVIAATE-2-(2,4-dinitrophenyl)aminoethylamide
2 - 620
2-aminobenzoyl-EPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
2 - 110
2-aminobenzoyl-GAMFLEAIPMSIP-2-(2,4-dinitrophenyl)aminoethylamide
2 - 280
2-aminobenzoyl-GPLELEEAQ-2-(2,4-dinitrophenyl)aminoethylamide
2 - 390
2-aminobenzoyl-GPLGLERAQ-2-(2,4-dinitrophenyl)aminoethylamide
2 - 660
2-aminobenzoyl-GPLGLREAQ-2-(2,4-dinitrophenyl)aminoethylamide
2 - 190
2-aminobenzoyl-PLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
2 - 110
2-aminobenzoyl-PLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
2 - 32
2-aminobenzoyl-RGLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
2 - 140
2-aminobenzoyl-RNALAVERTAS-2-(2,4-dinitrophenyl)aminoethylamide
-
6.2 - 1600
2-aminobenzoyl-RPLALEESQ-2-(2,4-dinitrophenyl)aminoethylamide
2 - 730
2-aminobenzoyl-RPLALRRSQ-2-(2,4-dinitrophenyl)aminoethylamide
2 - 420
2-aminobenzoyl-RPLALWEEQ-2-(2,4-dinitrophenyl)aminoethylamide
2 - 560
2-aminobenzoyl-RPLALWESQ-2-(2,4-dinitrophenyl)aminoethylamide
8.4 - 920
2-aminobenzoyl-RPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
2.3 - 760
2-aminobenzoyl-RPLELWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
2 - 720
2-aminobenzoyl-RPLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
2 - 310
2-aminobenzoyl-RPLGLGAAQ-2-(2,4-dinitrophenyl)aminoethylamide
2 - 59
2-aminobenzoyl-RPLGLGGAQ-2-(2,4-dinitrophenyl)aminoethylamide
2 - 700
2-aminobenzoyl-RPLGLWGAQ-2-(2,4-dinitrophenyl)aminoethylamide
34.6
DQ-collagen I
-
pH 7.5, 25°C
-
29.2
DQ-collagen IV
-
pH 7.5, 25°C
-
9.8
elastin fELN-125
-
pH 7.5, 25°C
-
51.57 - 159.7
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
55.4
triple helical peptide alpha1(V)
-
pH 7.5, 25°C
-
2
2-aminobenzoyl-ASVATELRAQ-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-ASVATELRAQ-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-ASVATELRAQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
170
2-aminobenzoyl-ASVATELRAQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-EAAPSSVIAATE-2-(2,4-dinitrophenyl)aminoethylamide
below, full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-EAAPSSVIAATE-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-EAAPSSVIAATE-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
50
2-aminobenzoyl-EAAPSSVIAATE-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-EPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
4.7
2-aminobenzoyl-EPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
69
2-aminobenzoyl-EPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
620
2-aminobenzoyl-EPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-GAMFLEAIPMSIP-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
5.9
2-aminobenzoyl-GAMFLEAIPMSIP-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
17
2-aminobenzoyl-GAMFLEAIPMSIP-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
110
2-aminobenzoyl-GAMFLEAIPMSIP-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-GPLELEEAQ-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
3.2
2-aminobenzoyl-GPLELEEAQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
3.6
2-aminobenzoyl-GPLELEEAQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
280
2-aminobenzoyl-GPLELEEAQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-GPLGLERAQ-2-(2,4-dinitrophenyl)aminoethylamide
below, full-length enzyme MMP-12, pH 7.5, 30°C
11
2-aminobenzoyl-GPLGLERAQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
38
2-aminobenzoyl-GPLGLERAQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
390
2-aminobenzoyl-GPLGLERAQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-GPLGLREAQ-2-(2,4-dinitrophenyl)aminoethylamide
below, full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-GPLGLREAQ-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
24
2-aminobenzoyl-GPLGLREAQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
660
2-aminobenzoyl-GPLGLREAQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-PLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
7.4
2-aminobenzoyl-PLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
27
2-aminobenzoyl-PLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
190
2-aminobenzoyl-PLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-PLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
6.2
2-aminobenzoyl-PLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
10
2-aminobenzoyl-PLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
110
2-aminobenzoyl-PLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-RGLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
below, full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-RGLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-RGLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
32
2-aminobenzoyl-RGLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-RNALAVERTAS-2-(2,4-dinitrophenyl)aminoethylamide
below, full-length enzyme MMP-12, pH 7.5, 30°C
-
2
2-aminobenzoyl-RNALAVERTAS-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
-
2
2-aminobenzoyl-RNALAVERTAS-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
-
140
2-aminobenzoyl-RNALAVERTAS-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
-
6.2
2-aminobenzoyl-RPLALEESQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
13
2-aminobenzoyl-RPLALEESQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
61
2-aminobenzoyl-RPLALEESQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
1600
2-aminobenzoyl-RPLALEESQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-RPLALRRSQ-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
7.3
2-aminobenzoyl-RPLALRRSQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
71
2-aminobenzoyl-RPLALRRSQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
730
2-aminobenzoyl-RPLALRRSQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-RPLALWEEQ-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
7.4
2-aminobenzoyl-RPLALWEEQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
74
2-aminobenzoyl-RPLALWEEQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
420
2-aminobenzoyl-RPLALWEEQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-RPLALWESQ-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
74
2-aminobenzoyl-RPLALWESQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
145
2-aminobenzoyl-RPLALWESQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
560
2-aminobenzoyl-RPLALWESQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
8.4
2-aminobenzoyl-RPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
10
2-aminobenzoyl-RPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
82
2-aminobenzoyl-RPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
920
2-aminobenzoyl-RPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
2.3
2-aminobenzoyl-RPLELWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
6
2-aminobenzoyl-RPLELWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
37
2-aminobenzoyl-RPLELWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
760
2-aminobenzoyl-RPLELWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-RPLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
8.5
2-aminobenzoyl-RPLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
64
2-aminobenzoyl-RPLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
720
2-aminobenzoyl-RPLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-RPLGLGAAQ-2-(2,4-dinitrophenyl)aminoethylamide
below, full-length enzyme MMP-12, pH 7.5, 30°C
2.7
2-aminobenzoyl-RPLGLGAAQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
23
2-aminobenzoyl-RPLGLGAAQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
310
2-aminobenzoyl-RPLGLGAAQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-RPLGLGGAQ-2-(2,4-dinitrophenyl)aminoethylamide
below, full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-RPLGLGGAQ-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
9.3
2-aminobenzoyl-RPLGLGGAQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
59
2-aminobenzoyl-RPLGLGGAQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
2
2-aminobenzoyl-RPLGLWGAQ-2-(2,4-dinitrophenyl)aminoethylamide
below, recombinant catalytic domain of MMP-12, pH 7.5, 30°C
3.9
2-aminobenzoyl-RPLGLWGAQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
55
2-aminobenzoyl-RPLGLWGAQ-2-(2,4-dinitrophenyl)aminoethylamide
recombinant catalytic domain of MMP-12, pH 7.5, 30°C
700
2-aminobenzoyl-RPLGLWGAQ-2-(2,4-dinitrophenyl)aminoethylamide
full-length enzyme MMP-12, pH 7.5, 30°C
0.59
fEln-100
-
pH 7.5, 25°C, mutant D124Q/M156E/A182G
-
0.82
fEln-100
-
pH 7.5, 25°C, mutant D124Q/M156E/I180S
-
1.31
fEln-100
-
pH 7.5, 25°C, mutant M156E/I180S
-
1.66
fEln-100
-
pH 7.5, 25°C, mutant D124Q/A182G
-
1.855
fEln-100
-
pH 7.5, 25°C, mutant D124Q/I180S
-
2.86
fEln-100
-
pH 7.5, 25°C, mutant I180S
-
3.57
fEln-100
-
pH 7.5, 25°C, mutant D124Q/M156E/F185Y
-
4.21
fEln-100
-
pH 7.5, 25°C, mutant D124Q/M156E
-
4.5
fEln-100
-
pH 7.5, 25°C, mutant D124Q/M156E/T205K
-
4.65
fEln-100
-
pH 7.5, 25°C, mutant M156E/A182G
-
4.89
fEln-100
-
pH 7.5, 25°C, mutant M156E
-
4.97
fEln-100
-
pH 7.5, 25°C, mutant A182G
-
7.06
fEln-100
-
pH 7.5, 25°C, mutant D124Q
-
7.13
fEln-100
-
pH 7.5, 25°C, mutant R117S
-
8.04
fEln-100
-
pH 7.5, 25°C, mutant M103F
-
10.69
fEln-100
-
pH 7.5, 25°C, wild-type
-
51.57
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/M156E/A182G
53.66
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/M156E/I180S
54.61
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/A182G
57.42
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant M156E/I180S
67.23
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/I180S
120.1
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant A182G
120.8
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant R117S
133.4
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/M156E/F185Y
133.8
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C
133.8
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, wild-type
134.7
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/M156E
135.2
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant M156E
136.7
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q
141.8
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant I180S
145.4
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant M156E/A182G
146.3
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant M103F
159.7
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
-
pH 7.5, 25°C, mutant D124Q/M156E/T205K
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A164V
-
mutation inconsequential to elastolysis
A182G
-
mutant retains similar activity toward substrate MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 (Km and kcat similar to wild-type, kcat/Km), mutant shows strong decreased (kcat/Km) toward fEln-100 compared to wild-type
D124Q
-
mutant retains similar activity toward substrate MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 (Km and kcat similar to wild-type, kcat/Km), mutant shows decreased (kcat/Km) toward fEln-100 compared to wild-type
D124Q/A182G
-
combination of two well-separated mutations further reduces activity toward both fEln-100 and elastin-fluorescein compared to the single mutations, mutant shows decreased activity towards MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
D124Q/I180S
-
combination of two well-separated mutations further reduces activity toward both fEln-100 and elastin-fluorescein compared to the single mutations, mutant shows decreased activity towards MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
D124Q/M156E
-
combination of two well-separated mutations further reduces activity toward both fEln-100 and elastin-fluorescein compared to the single mutations, mutant retains wild-type activity towards MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
D124Q/M156E/A182G
-
mutant confers a significantly greater loss of catalytic efficiency in digesting fEln-100 than the parental double mutant D124Q/M156E, catalytic activity toward MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 is highly decreased compared to wild-type, compared to triple mutant D124Q/M156E/F185Y and D124Q/M156E/T205K catalytic efficacy toward fEln-100 is highly decreased
D124Q/M156E/F185Y
-
mutant confers a significantly greater loss of catalytic efficiency in digesting fEln-100 than the parental double mutant D124Q/M156E, catalytic activity toward MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 is not affected compared to wild-type, compared to triple mutant D124Q/M156E/I180S and D124Q/M156E/A182G catalytic efficacy toward fEln-100 is moderately decreased
D124Q/M156E/I180S
-
mutant confers a significantly greater loss of catalytic efficiency in digesting fEln-100 than the parental double mutant D124Q/M156E, catalytic activity toward MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 is highly decreased compared to wild-type, compared to triple mutant D124Q/M156E/F185Y and D124Q/M156E/T205K catalytic efficacy toward fEln-100 is highly decreased
D124Q/M156E/T205K
-
mutant confers a significantly greater loss of catalytic efficiency in digesting fEln-100 than the parental double mutant D124Q/M156E, catalytic activity toward MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 is not affected compared to wild-type, compared to triple mutant D124Q/M156E/I180S and D124Q/M156E/A182G catalytic efficacy toward fEln-100 is moderately decreased
D200E
-
mutation inconsequential to elastolysis
G166R
-
mutation inconsequential to elastolysis
I180S
-
mutant retains similar activity toward substrate MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 (Km and kcat similar to wild-type, kcat/Km), mutant shows strong decreased (kcat/Km) toward fEln-100 compared to wild-type
I255V
-
mutation inconsequential to elastolysis
K148T
-
mutation inconsequential to elastolysis
M103F
-
mutant retains similar activity toward substrate MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 (Km and kcat similar to wild-type, kcat/Km), mutant shows decreased catalytic efficacy (kcat/Km) toward fEln-100 compared to wild-type
M156E
-
mutant retains similar activity toward substrate MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 (Km and kcat similar to wild-type, kcat/Km), mutant shows strong decreased (kcat/Km) toward fEln-100 compared to wild-type
M156E/A182G
-
kcat (fEln-100) is twice that of wild-type, mutant retains wild-type activity towards MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
M156E/I180S
-
combination of two well-separated mutations further reduces activity toward both fEln-100 and elastin-fluorescein compared to the single mutations, mutant shows decreased activity towards MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
N153Y
-
mutation inconsequential to elastolysis
R117S
-
mutant retains similar activity toward substrate MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 (Km and kcat similar to wild-type, kcat/Km), mutant shows decreased (kcat/Km) toward fEln-100 compared to wild-type
S142E
-
mutation inconsequential to elastolysis
V144A
-
mutation inconsequential to elastolysis
V162S
-
mutation inconsequential to elastolysis
Y132A
-
mutation inconsequential to elastolysis
E219A
-
site-directed mutagenesis, inactive mutant, autolysis of the mutant is prevented
E219A
-
NMR studies used MMP-12 preserved by E219A substitution of the general base
additional information
-
MMP-12 knockout mice, no mucosal damage when trinitrobenzene sulfonic acid is administered to the colons compared to severe colitis in wild type mice
additional information
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administration of trinitrobenzene sulphonic acid to the colons of MMP-12 knockout mice for 7 days does not lead to mucosal damage in contrast to wild-type mice which show severe colitis, overview
additional information
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construction of a mutant peptide identical to SR-20, i.e. 344-SRNQLFLFKDEKYWLINNLV-363, except that the Lys-Asp-Glu-Lys motif found in mouse MMP12 is replaced by the human MMP9 sequence, Ser-Gly-Arg-Gln. The Lys-Asp-Glu-Lys motif is essential for the antimicrobial properties of mouse MMP12 C-terminal domain. Mmp12-/- mice exhibit impaired bacterial clearance and increased mortality when challenged with both Gram-negative and Gram-positive bacteria at macrophage-rich portals of entry, such as the peritoneum and lung
additional information
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development of pulmonary fibrosis in MMP-12 -/- knockout mice
additional information
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mice lacking MMP12 have impaired ability to destroy bacteria in the phagolysosomes and die as a result of uncontrolled spread of the infection. The increased mortality is observed when the bacteria are injected through the airway, but not when the bacteria are injected into the blood
additional information
gene ration of enzyme-deficient mutant betaENaC-overexpressing mice, betaENaC-Tg/MMP12-/- mice
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Homo sapiens
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