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Information on EC 3.4.24.65 - macrophage elastase and Organism(s) Homo sapiens and UniProt Accession P45452

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.65 macrophage elastase
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P45452 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at -Ala14-/-Leu- and -Tyr16-/-Leu- in the B chain of insulin
Synonyms
mmp-12, mmp12, matrix metalloproteinase-12, macrophage elastase, matrix metalloproteinase 12, metalloelastase, macrophage metalloelastase, human macrophage metalloelastase, hmmp-12, mouse macrophage metalloelastase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Metalloelastase
-
hMMP-12
-
-
human macrophage elastase
-
-
Human macrophage metalloelastase
human metalloelastase
-
-
Macrophage elastase
macrophage matrix metalloproteinase
-
-
macrophage metalloelastase
-
-
macrophage-specific metalloelastase
-
-
matrix metalloproteinase 12
-
-
Matrix metalloproteinase-12
Metalloelastase
MME
-
-
-
-
MMP-12
MMP12
-
-
rHME
-
-
additional information
-
MMP-12 is a member of the family of matrix metalloproteinases, MMPs
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
146888-86-0
-
150680-47-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,4-dinitrophenyl-Arg-Pro-Leu-Ala-Ala-Trp-Arg-Ser-NH2 + H2O
?
show the reaction diagram
-
-
-
?
2,4-dinitrophenyl-Arg-Pro-Leu-Ala-Arg-Trp-Arg-Ser-NH2 + H2O
?
show the reaction diagram
-
-
-
?
2,4-dinitrophenyl-Arg-Pro-Leu-Ala-Glu-Trp-Arg-Ser-NH2 + H2O
?
show the reaction diagram
-
-
-
?
2,4-dinitrophenyl-Arg-Pro-Leu-Ala-Leu-Trp-Arg-Ser-NH2 + H2O
?
show the reaction diagram
-
-
-
?
2,4-dinitrophenyl-Arg-Pro-Leu-Ala-Lys-Trp-Arg-Ser-NH2 + H2O
?
show the reaction diagram
-
-
-
?
2,4-dinitrophenyl-Arg-Pro-Leu-Ala-Phe-Trp-Arg-Ser-NH2 + H2O
?
show the reaction diagram
-
-
-
?
2,4-dinitrophenyl-Arg-Pro-Leu-Ala-Ser-Trp-Arg-Ser-NH2 + H2O
?
show the reaction diagram
-
-
-
?
2,4-dinitrophenyl-Arg-Pro-Leu-Ala-Trp-Trp-Arg-Ser-NH2 + H2O
?
show the reaction diagram
-
-
-
?
2,4-dinitrophenyl-Arg-Pro-Leu-Ala-Tyr-Trp-Arg-Ser-NH2 + H2O
?
show the reaction diagram
-
-
-
?
2-aminobenzoyl-ASVATELRAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-ASVATE + LRAQ-2-(2,4-dinitrophenyl)aminoethylamide
show the reaction diagram
-
-
-
?
2-aminobenzoyl-EAAPSSVIAATE-2-(2,4-dinitrophenyl)aminoethylamide + H2O
?
show the reaction diagram
-
-
-
?
2-aminobenzoyl-EPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-EPLA + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
show the reaction diagram
minor cleavage site is E-/-PLA
-
-
?
2-aminobenzoyl-GAMFLEAIPMSIP-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-GAMF + LEAIPMSIP-2-(2,4-dinitrophenyl)aminoethylamide
show the reaction diagram
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
show the reaction diagram
-
-
-
?
2-aminobenzoyl-GPLGLERAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-GPLG + LERAQ-2-(2,4-dinitrophenyl)aminoethylamide
show the reaction diagram
-
-
-
?
2-aminobenzoyl-GPLGLREAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-GPLG + LREAQ-2-(2,4-dinitrophenyl)aminoethylamide
show the reaction diagram
-
-
-
?
2-aminobenzoyl-PLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-PLA + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
show the reaction diagram
minor cleavage site is PL-/-A
-
-
?
2-aminobenzoyl-PLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-PLG + LEEA-2-(2,4-dinitrophenyl)aminoethylamide
show the reaction diagram
-
-
-
?
2-aminobenzoyl-RGLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RGLA + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
show the reaction diagram
minor cleavage site is LW-/-RSQ
-
-
?
2-aminobenzoyl-RNALAVERTAS-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RNALA + VERTAS-2-(2,4-dinitrophenyl)aminoethylamide
show the reaction diagram
-
-
-
?
2-aminobenzoyl-RPLALEESQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LEESQ-2-(2,4-dinitrophenyl)aminoethylamide
show the reaction diagram
-
-
-
?
2-aminobenzoyl-RPLALRRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LRRSQ-2-(2,4-dinitrophenyl)aminoethylamide
show the reaction diagram
minor cleavage site is RPL-/-A
-
-
?
2-aminobenzoyl-RPLALWEEQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LWEEQ-2-(2,4-dinitrophenyl)aminoethylamide
show the reaction diagram
-
-
-
?
2-aminobenzoyl-RPLALWESQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LWESQ-2-(2,4-dinitrophenyl)aminoethylamide
show the reaction diagram
-
-
-
?
2-aminobenzoyl-RPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLA + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
show the reaction diagram
minor cleavage site is RPL-/-A
-
-
?
2-aminobenzoyl-RPLELWRSQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLE + LWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
show the reaction diagram
minor cleavage site is RPL-/-E
-
-
?
2-aminobenzoyl-RPLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLG + LEEA-2-(2,4-dinitrophenyl)aminoethylamide
show the reaction diagram
-
-
-
?
2-aminobenzoyl-RPLGLGAAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLG + LGAAQ-2-(2,4-dinitrophenyl)aminoethylamide
show the reaction diagram
-
-
-
?
2-aminobenzoyl-RPLGLGGAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLG + LGGAQ-2-(2,4-dinitrophenyl)aminoethylamide
show the reaction diagram
-
-
-
?
2-aminobenzoyl-RPLGLWGAQ-2-(2,4-dinitrophenyl)aminoethylamide + H2O
2-aminobenzoyl-RPLG + LWGAQ-2-(2,4-dinitrophenyl)aminoethylamide
show the reaction diagram
minor cleavage site is RPL-/-G
-
-
?
alpha-1-antitrypsin + H2O
?
show the reaction diagram
-
recombinant enzyme rHME
-
?
alpha1-antitrypsin + H2O
?
show the reaction diagram
-
-
-
-
?
beta-casein + H2O
?
show the reaction diagram
-
-
-
-
?
chondroitan sulfate + H2O
?
show the reaction diagram
-
recombinant enzyme rHME
-
?
Collagen type I + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
DQ-collagen IV + H2O
?
show the reaction diagram
-
-
-
-
?
Elastin + H2O
?
show the reaction diagram
elastin fELN-125 + H2O
?
show the reaction diagram
-
-
-
-
?
enactin + H2O
?
show the reaction diagram
-
recombinant enzyme rHME
-
?
extracellular matrix protein + H2O
?
show the reaction diagram
-
may be required for macrophages to penetrate basement membranes and remodel injured tissue during inflammation
-
?
fEln-100 + H2O
?
show the reaction diagram
-
alpha-elastin
-
-
?
Fibronectin + H2O
?
show the reaction diagram
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
heparan sulfate + H2O
?
show the reaction diagram
-
recombinant enzyme rHME
-
?
Laminin + H2O
?
show the reaction diagram
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
show the reaction diagram
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
Mca-Pro-Leu-Gly + Leu-Dpa-Ala-Arg-NH2
show the reaction diagram
-
-
-
-
?
Mca-Pro-Leu-Gly-Leu-Glu-Glu-Ala-Dpa-NH2 + H2O
Mca-Pro-Leu-Gly + Leu-Glu-Glu-Ala-Dpa-NH2
show the reaction diagram
-
selective cleavage, the Glu-Glu motif interacts with the S'2 and S'3 subsites of MMP-12
-
-
?
TNF-alpha + H2O
?
show the reaction diagram
-
-
-
-
?
triple helical peptide alpha1(V) + H2O
?
show the reaction diagram
-
collagen V fibrils
-
-
?
Type IV collagen + H2O
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Elastin + H2O
?
show the reaction diagram
extracellular matrix protein + H2O
?
show the reaction diagram
-
may be required for macrophages to penetrate basement membranes and remodel injured tissue during inflammation
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
batimastat
BB-94
(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
-
-
alpha2-Macroglobulin
-
SDS abolishes inhibition
-
CGS-27023A
-
a hydroxamate inhibitor
CGS27023A
-
-
dexamethasone
-
in vivo inhibition of the human enzyme in mice leading to inhibited cytokine release and neutrophil influx, overview
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-[3-[(4-bromophenyl)(hydroxy)phosphoryl]-2-[3-(3'-chlorobiphenyl-4-yl)isoxazol-5-yl]propanoyl]-L-alpha-glutamyl-L-alpha-glutamine
-
-
rolipram
-
in vivo inhibition of the human enzyme in mice leading to inhibited neutrophil influx, overview
tissue inhibitor of metalloproteinase
-
i.e. TIMP-1, recombinant enzyme
-
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
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.001 - 0.021
fEln-100
-
6.8 - 24.1
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 170
2-aminobenzoyl-ASVATELRAQ-2-(2,4-dinitrophenyl)aminoethylamide
2 - 50
2-aminobenzoyl-EAAPSSVIAATE-2-(2,4-dinitrophenyl)aminoethylamide
69 - 620
2-aminobenzoyl-EPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
17 - 110
2-aminobenzoyl-GAMFLEAIPMSIP-2-(2,4-dinitrophenyl)aminoethylamide
3.6 - 280
2-aminobenzoyl-GPLELEEAQ-2-(2,4-dinitrophenyl)aminoethylamide
11 - 390
2-aminobenzoyl-GPLGLERAQ-2-(2,4-dinitrophenyl)aminoethylamide
24 - 660
2-aminobenzoyl-GPLGLREAQ-2-(2,4-dinitrophenyl)aminoethylamide
27 - 190
2-aminobenzoyl-PLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
10 - 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
-
61 - 1600
2-aminobenzoyl-RPLALEESQ-2-(2,4-dinitrophenyl)aminoethylamide
71 - 730
2-aminobenzoyl-RPLALRRSQ-2-(2,4-dinitrophenyl)aminoethylamide
74 - 420
2-aminobenzoyl-RPLALWEEQ-2-(2,4-dinitrophenyl)aminoethylamide
74 - 560
2-aminobenzoyl-RPLALWESQ-2-(2,4-dinitrophenyl)aminoethylamide
82 - 920
2-aminobenzoyl-RPLALWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
37 - 760
2-aminobenzoyl-RPLELWRSQ-2-(2,4-dinitrophenyl)aminoethylamide
64 - 720
2-aminobenzoyl-RPLGLEEA-2-(2,4-dinitrophenyl)aminoethylamide
23 - 310
2-aminobenzoyl-RPLGLGAAQ-2-(2,4-dinitrophenyl)aminoethylamide
9.3 - 59
2-aminobenzoyl-RPLGLGGAQ-2-(2,4-dinitrophenyl)aminoethylamide
55 - 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
-
0.59 - 10.69
fEln-100
-
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
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000044
N-(3-[(4-bromophenyl)(hydroxy)phosphoryl]-2-[3-[4-(dimethylamino)phenyl]isoxazol-5-yl]propanoyl)-L-alpha-glutamyl-L-alpha-glutamine
-
-
0.00000019
N-[3-[(4-bromophenyl)(hydroxy)phosphoryl]-2-[3-(3'-chlorobiphenyl-4-yl)isoxazol-5-yl]propanoyl]-L-alpha-glutamyl-L-alpha-glutamine
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
149
(1S,5S,7R)-3-aza-6,8-dioxa-bicyclo[3.2.1]octane-3,7-dicarboxylic acid 7-[(biphenyl-4-ylmethyl)-amide] 3-hydroxyamide
Homo sapiens
-
pH 7.0, 25°C, recombinant enzyme
0.954
(1S,5S,7R)-3-biphenyl-4-ylmethyl-2-oxo-3-aza-6,8-dioxa-bicyclo[3.2.1]octane-7-carboxylic acid
Homo sapiens
-
pH 7.0, 25°C, recombinant enzyme
425
(1S,5S,7R)-3-biphenyl-4-ylmethyl-2-oxo-3-aza-6,8-dioxa-bicyclo[3.2.1]octane-7-carboxylic acid hydroxyamide
Homo sapiens
-
pH 7.0, 25°C, recombinant enzyme
835
(1S,5S,7R)-3-biphenyl-4-ylmethyl-3-aza-6,8-dioxabicyclo[3.2.1]octane-7-carboxylic acid
Homo sapiens
-
pH 7.0, 25°C, recombinant enzyme
399
(1S,5S,7R)-3-biphenyl-4-ylmethyl-3-aza-6,8-dioxabicyclo[3.2.1]octane-7-carboxylic acid hydroxyamide
Homo sapiens
-
pH 7.0, 25°C, recombinant enzyme
0.000024
(3R)-3-([[4-(4'-acetylbiphenyl-4-yl)-5-fluorothiophen-2-yl]carbonyl]amino)-3-phenylpropanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000013
(3R)-3-[([5-fluoro-4-[4-(pyridin-4-yl)phenyl]thiophen-2-yl]carbonyl)amino]-3-phenylpropanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0002
(3R)-3-[([5-fluoro-4-[4-(trifluoromethoxy)phenyl]thiophen-2-yl]carbonyl)amino]-3-phenylpropanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000085
N-[(1R)-3-amino-3-oxo-1-phenylpropyl]-5-fluoro-4-[4-(trifluoromethoxy)phenyl]thiophene-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000007
trans-4-[([[4-(4'-acetylbiphenyl-4-yl)-5-fluorothiophen-2-yl]carbonyl]amino)methyl]cyclohexanecarboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0036
trans-4-[[([3-[4-(trifluoromethoxy)phenyl]-1,2-thiazol-5-yl]carbonyl)amino]methyl]cyclohexanecarboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0004
trans-4-[[([4-[4-(trifluoromethoxy)phenyl]thiophen-2-yl]carbonyl)amino]methyl]cyclohexanecarboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00014
trans-4-[[([5-fluoro-4-[4-(trifluoromethoxy)phenyl]thiophen-2-yl]carbonyl)amino]methyl]cyclohexanecarboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.031
trans-4-[[([5-[4-(trifluoromethoxy)phenyl]-1,2-thiazol-3-yl]carbonyl)amino]methyl]cyclohexanecarboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
specific activity 265 cpm/microgram
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
assay at
7
-
assay at
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
30
assay at
33
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
human
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
subchondral
Manually annotated by BRENDA team
-
metalloproteinase 12 (MMP-12) is induced in chondrocytes during fetal development and malignant transformation
Manually annotated by BRENDA team
-
bronchial
Manually annotated by BRENDA team
-
HME protein levels are 4.50-7.15fold increased in gastric carcinoma samples compared with the non-cancerous controls
Manually annotated by BRENDA team
-
16-50 SCCs, in situ detection, overview
Manually annotated by BRENDA team
-
HME is expressed in chronic gastritis with atypical hyperplasia and normal gastric epithelium mucosa. HME protein levels are 4.50-7.15fold increased in gastric carcinoma samples compared with the non-cancerous controls
Manually annotated by BRENDA team
-
mainly expressed by inflammatory macrophages in the rhematoid arthritis synovial membrane. Rheumatoid synovial tissue contains higher levels of MMP-12 messenger RNA than does osteoarthritis synovial tissue. Macrophage-derived MMP-12 may play an important role in the destructive process in rheumatoid arthritis
Manually annotated by BRENDA team
additional information
-
enzyme expression analysis in bones and cartilage of healthy subjects and patients with osteoarthritis (OA), overview. During disease progression, MMP-12 is expressed at the sides of the cartilage and bone erosion and in the bone cysts. Furthermore, it is traced in the osteocytes of the subchondral bone. Osteoblast-like cells and bone lining cells express MMP-12 during the stage of severe OA. MMP-12 expression is positively correlated with the age and the BMI of OA patients
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
recombinant enzyme from Escherichia coli
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
degradation of elastin is central to the pathogenesis of emphysema
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MMP13_HUMAN
471
0
53820
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22000
29000
-
x * 54000, pro-MMP-12, x * 29000, mature active MMP-12
45000
-
MMp-12 active enzyme
54000
additional information
-
the open-reading frames predict proenzymes of MW 54000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
-
-
proteolytic modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion technique, crystallized in complex with inhibitor batimastat, BB-94, monoclinic space group C2, crystal cell constants a : 51.91 A, b : 60.26 A, c : 54.61 A
hexagonal shaped crystals, crystal structure in complex with hydroxamic acid inhibitor, orthorhombic space group I222, unit cells dimensions a : 67.4 A, b : 87.2, c : 169.2
-
purified MMP-12 bound to hydroxamic acid, hanging drop vapour diffusion method, 20°C, from protein solution containing 10 mg/ml protein in 0.1 M Tris-HCl, pH 8.0, 30% PEG 6000, 200 mM hydroxamic acid, and 1.0 M LiCl, a few days, X-ray diffraction structure determination and analysis at 1.3 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
E219A
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
catalytic domain of MMP-12 exhibits higher activity, more rigidity of its backbone, and lower folding stability than its counterpart of the MMP-3 catalytic domain that has more internal motions throughout
-
Purification in the presence of EDTA prevents activation of proenzyme
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial, recombinant or native enzyme
-
recombinant C-terminally His-tagged catalytic domain of MMP-12 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and desalting gel filtration
recombinant F171D mutant fragment Gly106-Gly263 from Escherichia coli strain BL21 by gel filtration and anion exchange chromatography
-
refolded recombinant MMP-12 catalytic domain from Escherichia coli strain BL21(DE3) inclusion bodies by anion exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
MMP-12 catalytic domain, cd(EA)MMP-12 overexpressed in Escherichia coli strain BL21 (DE3)
cloned and expressed in Escherichia coli BL21(DE3)
-
expressed in Escherichia coli
-
expression analysis
-
expression analysis of MMP12 in cancerous and healthy oral tissues, overview
-
expression of a cDNA encoding the fragment Gly106-Gly263 of the enzyme F171D mutant in Escherichia coli strain BL21
-
generation of transgenic rabbits that express human (h)MMP-12 gene under the control of a macrophage-specific promoter, the human scavenger receptor promoter. This transgenic rabbit model with increased expression of hMMP-12 may become a useful model for further mechanistic studies of MMP-12 in in inflammatory diseases and cancer invasion, it is also an ideal model for testing the in vivo action of MMP-12 inhibitors
-
molecular cloning of the proteinase domain of MMP12
-
overexpression of the MMP-12 catalytic domain, residues Phe100-Gly263, in Escherichia coli strain BL21(DE3) inclusion bodies
-
recombinant expression of C-terminally His-tagged catalytic domain of MMP-12 in Escherichia coli strain BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
metalloproteinase 12 (MMP-12) is induced in chondrocytes during fetal development and malignant transformation
-
MMP-12 expression is upregulated by other matrix components such as hyaluronan fragments, cytokines, and growth factors, for example by TGF-beta, IFN-gamma and EGF, and serine proteases such as thrombin and plasmin
-
UV radiation is known to induce the expression of MMP-12 in skin
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant fragment of mutant F171D from Escherichia coli inclusion bodies by solubilization in 20 mM Tris-HCl and 8 M urea at pH 8.0, refolding by multi-step dialysis, overview
-
recombinant MMP-12 catalytic domain from Escherichia coli strain BL21(DE3) inclusion bodies with refolding buffer, which contains 6 M urea, 20 mM Tris-HCl, 5 mM CaCl2, and 100 mM NaCl, pH 7.5, followed by a two-step dialysis against refolding buffer containing 0.1 mM ZnCl2, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
the enzyme can be utilized for pharmacological evaluation of anti-inflammatory mechanisms of action
diagnostics
drug development
medicine
pharmacology
-
MMP-12 plays a predominant role in the inflammatory process induced by cigarette smoke, and therefore is potentially an important therapeutic target for the treatment of chronic obstructive pulmonary diseases
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shapiro, S.D.; Kobayashi, D.K.; Ley, T.J.
Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages
J. Biol. Chem.
268
23824-23829
1993
Homo sapiens
Manually annotated by BRENDA team
Gronski, T.J., Jr.; Martin, R.L.; Kobayashi, D.K.; Walsh, B.C.; Holman, M.C.; Huber, M.; Van Wart, H.E.; Shapiro, S.D.
Hydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastase
J. Biol. Chem.
272
12189-12194
1997
Homo sapiens
Manually annotated by BRENDA team
Lang, R.; Kocourek, A.; Braun, M.; Tschesche, H.; Huber, R.; Bode, W.; Maskos, K.
Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 A crystal structure
J. Mol. Biol.
312
731-742
2001
Homo sapiens (P45452), Homo sapiens
Manually annotated by BRENDA team
Nar, H.; Werle, K.; Bauer, M.M.; Dollinger, H.; Jung, B.
Crystal structure of human macrophage elastase (MMP-12) in complex with a hydroxamic acid inhibitor
J. Mol. Biol.
312
743-751
2001
Homo sapiens
Manually annotated by BRENDA team
Liu, M.; Sun, H.; Wang, X.; Koike, T.; Mishima, H.; Ikeda, K.; Watanabe, T.; Ochiai, N.; Fan, J.
Association of increased expression of macrophage elastase (matrix metalloproteinase 12) with rheumatoid arthritis
Arthritis Rheum.
50
3112-3117
2004
Homo sapiens
Manually annotated by BRENDA team
Liang, J.; Liu, E.; Yu, Y.; Kitajima, S.; Koike, T.; Jin, Y.; Morimoto, M.; Hatakeyama, K.; Asada, Y.; Watanabe, T.; Sasaguri, Y.; Watanabe, S.; Fan, J.
Macrophage metalloelastase accelerates the progression of atherosclerosis in transgenic rabbits
Circulation
113
1993-2001
2006
Homo sapiens
Manually annotated by BRENDA team
Molet, S.; Belleguic, C.; Lena, H.; Germain, N.; Bertrand, C.P.; Shapiro, S.D.; Planquois, J.M.; Delaval, P.; Lagente, V.
Increase in macrophage elastase (MMP-12) in lungs from patients with chronic obstructive pulmonary disease
Inflamm. Res.
54
31-36
2005
Homo sapiens
Manually annotated by BRENDA team
Fan, J.; Wang, X.; Wu, L.; Matsumoto, S.I.; Liang, J.; Koike, T.; Ichikawa, T.; Sun, H.; Shikama, H.; Sasaguri, Y.; Watanabe, T.
Macrophage-specific overexpression of human matrix metalloproteinase-12 in transgenic rabbits
Transgenic Res.
13
261-269
2004
Homo sapiens
Manually annotated by BRENDA team
Mannino, C.; Nievo, M.; Machetti, F.; Papakyriakou, A.; Calderone, V.; Fragai, M.; Guarna, A.
Synthesis of bicyclic molecular scaffolds (BTAa): an investigation towards new selective MMP-12 inhibitors
Bioorg. Med. Chem.
14
7392-7403
2006
Homo sapiens
Manually annotated by BRENDA team
Nenan, S.; Lagente, V.; Planquois, J.M.; Hitier, S.; Berna, P.; Bertrand, C.P.; Boichot, E.
Metalloelastase (MMP-12) induced inflammatory response in mice airways: effects of dexamethasone, rolipram and marimastat
Eur. J. Pharmacol.
559
75-81
2007
Homo sapiens
Manually annotated by BRENDA team
Nenan, S.; Boichot, E.; Planquois, J.M.; Berna, P.; Hitier, S.; Benard, T.; Lagente, V.; Bertrand, C.P.
Effects of depletion of neutrophils or macrophages on the inflammatory response induced by metalloelastase (MMP-12) in mice airways
Eur. J. Pharmacol.
579
374-381
2008
Homo sapiens
Manually annotated by BRENDA team
Devel, L.; Rogakos, V.; David, A.; Makaritis, A.; Beau, F.; Cuniasse, P.; Yiotakis, A.; Dive, V.
Development of selective inhibitors and substrate of matrix metalloproteinase-12
J. Biol. Chem.
281
11152-11160
2006
Homo sapiens
Manually annotated by BRENDA team
Bhaskaran, R.; Palmier, M.O.; Bagegni, N.A.; Liang, X.; Van Doren, S.R.
Solution structure of inhibitor-free human metalloelastase (MMP-12) indicates an internal conformational adjustment
J. Mol. Biol.
374
1333-1344
2007
Homo sapiens
Manually annotated by BRENDA team
Taddese, S.; Weiss, A.S.; Neubert, R.H.; Schmelzer, C.E.
Mapping of macrophage elastase cleavage sites in insoluble human skin elastin
Matrix Biol.
27
420-428
2008
Homo sapiens
Manually annotated by BRENDA team
Zheng, X.; Ou, L.; Tong, X.; Zhu, J.; Wu, H.
Over-expression and refolding of isotopically labeled recombinant catalytic domain of human macrophage elastase (MMP-12) for NMR studies
Protein Expr. Purif.
56
160-166
2007
Homo sapiens
Manually annotated by BRENDA team
Yen, C.Y.; Chen, C.H.; Chang, C.H.; Tseng, H.F.; Liu, S.Y.; Chuang, L.Y.; Wen, C.H.; Chang, H.W.
Matrix metalloproteinases (MMP) 1 and MMP10 but not MMP12 are potential oral cancer markers
Biomarkers
14
244-249
2009
Homo sapiens
Manually annotated by BRENDA team
Cheng, P.; Jiang, F.H.; Zhao, L.M.; Dai, Q.; Yang, W.Y.; Zhu, L.M.; Wang, B.J.; Xu, C.; Bao, Y.J.; Zhang, Y.J.
Human macrophage metalloelastase correlates with angiogenesis and prognosis of gastric carcinoma
Digest. Dis. Sci.
55
3138-3146
2010
Homo sapiens
Manually annotated by BRENDA team
Boyd, S.; Virolainen, S.; Paerssinen, J.; Skoog, T.; van Hogerlinden, M.; Latonen, L.; Kylloenen, L.; Toftgard, R.; Saarialho-Kere, U.
MMP-10 (Stromelysin-2) and MMP-21 in human and murine squamous cell cancer
Exp. Dermatol.
18
1044-1052
2009
Homo sapiens
Manually annotated by BRENDA team
Lagente, V.; Le Quement, C.; Boichot, E.
Macrophage metalloelastase (MMP-12) as a target for inflammatory respiratory diseases
Expert Opin. Ther. Targets
13
287-295
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Kaner, R.J.; Santiago, F.; Crystal, R.G.
Up-regulation of alveolar macrophage matrix metalloproteinases in HIV1(+) smokers with early emphysema
J. Leukoc. Biol.
86
913-922
2009
Homo sapiens
Manually annotated by BRENDA team
Fulcher, Y.G.; Van Doren, S.R.
Remote exosites of the catalytic domain of matrix metalloproteinase-12 enhance elastin degradation
Biochemistry
50
9488-9499
2011
Homo sapiens
Manually annotated by BRENDA team
Taddese, S.; Jung, M.; Ihling, C.; Heinz, A.; Neubert, R.; Schmelzer, C.
MMP-12 catalytic domain recognizes and cleaves at multiple sites in human skin collagen type I and type III
Biochim. Biophys. Acta
1804
731-739
2010
Homo sapiens
Manually annotated by BRENDA team
Badland, M.; Compere, D.; Courte, K.; Dublanchet, A.C.; Blais, S.; Manage, A.; Peron, G.; Wrigglesworth, R.
Thiophene and bioisostere derivatives as new MMP12 inhibitors
Bioorg. Med. Chem. Lett.
21
528-530
2011
Homo sapiens
Manually annotated by BRENDA team
Liang, X.; Arunima, A.; Zhao, Y.; Bhaskaran, R.; Shende, A.; Byrne, T.S.; Fleeks, J.; Palmier, M.O.; Van Doren, S.R.
Apparent tradeoff of higher activity in MMP-12 for enhanced stability and flexibility in MMP-3
Biophys. J.
99
273-283
2010
Homo sapiens
Manually annotated by BRENDA team
Urbschat, A.; Paulus, P.; Wiegratz, I.; Beschmann, H.; Hadji, P.; Hofmann, R.; Ochsendorf, F.
Macrophage metalloelastase-12 is detectable in human seminal plasma and represents a predictor for inflammatory processes in the male genital tract
Andrologia
47
153-159
2015
Homo sapiens (P39900), Homo sapiens
Manually annotated by BRENDA team
Lavilla-Alonso, S.; Bauer, M.; Abo-Ramadan, U.; Ristimki, A.; Halavaara, J.; Desmond, R.; Wang, D.; Escutenaire, S.; Ahtiainen, L.; Saksela, K.; Tatlisumak, T.; Hemminki, A.; Pesonen, S.
Macrophage metalloelastase (MME) as adjuvant for intra-tumoral injection of oncolytic adenovirus and its influence on metastases development
Cancer Gene Ther.
19
126-134
2012
Homo sapiens
Manually annotated by BRENDA team
Lamort, A.S.; Gravier, R.; Laffitte, A.; Juliano, L.; Zani, M.L.; Moreau, T.
New insights into the substrate specificity of macrophage elastase MMP-12
Biol. Chem.
397
469-484
2016
Mus musculus (P34960), Mus musculus, Homo sapiens (P39900), Homo sapiens
Manually annotated by BRENDA team
Kaspiris, A.; Khaldi, L.; Chronopoulos, E.; Vasiliadis, E.; Grivas, T.B.; Kouvaras, I.; Dagkas, S.; Papadimitriou, E.
Macrophage-specific metalloelastase (MMP-12) immunoexpression in the osteochondral unit in osteoarthritis correlates with BMI and disease severity
Pathophysiology
22
143-151
2015
Homo sapiens
Manually annotated by BRENDA team