3.4.24.65: macrophage elastase
This is an abbreviated version!
For detailed information about macrophage elastase, go to the full flat file.
Word Map on EC 3.4.24.65
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3.4.24.65
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metalloproteinases
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mmp-9
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pulmonary
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emphysema
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collagen
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alveolar
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elastin
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fibrosis
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smoke
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airway
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timp-1
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cigarette
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lavage
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bronchoalveolar
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endothelial
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metastasis
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aortic
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tnf
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artery
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chemokine
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monocyte
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smoking
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plaque
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aneurysm
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angiogenesis
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atherosclerotic
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zymography
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smoke-induced
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elastolytic
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proteinases
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plasminogen
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asthma
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rupture
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angiostatin
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bal
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instil
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urokinase-type
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matrilysin
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airspace
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mt1-mmp
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cs-induced
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elastases
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smoke-exposed
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emphysematous
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diagnostics
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drug development
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elastase-induced
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collagenase-3
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cs-exposed
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airflow
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medicine
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pharmacology
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matrix-degrading
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analysis
- 3.4.24.65
- metalloproteinases
- mmp-9
- pulmonary
- emphysema
- collagen
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alveolar
- elastin
- fibrosis
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smoke
- airway
- timp-1
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cigarette
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lavage
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bronchoalveolar
- endothelial
- metastasis
- aortic
- tnf
- artery
- chemokine
- monocyte
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smoking
- plaque
- aneurysm
- angiogenesis
- atherosclerotic
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zymography
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smoke-induced
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elastolytic
- proteinases
- plasminogen
- asthma
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rupture
- angiostatin
- bal
-
instil
-
urokinase-type
- matrilysin
-
airspace
- mt1-mmp
-
cs-induced
- elastases
-
smoke-exposed
-
emphysematous
- diagnostics
- drug development
-
elastase-induced
- collagenase-3
-
cs-exposed
-
airflow
- medicine
- pharmacology
-
matrix-degrading
- analysis
Reaction
Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at -Ala14-/-Leu- and -Tyr16-/-Leu- in the B chain of insulin =
Synonyms
HME, 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, ME, Metalloelastase, MME, MMP-12, MMP12, More, mouse macrophage metalloelastase, rHME
ECTree
Advanced search results
Engineering
Engineering on EC 3.4.24.65 - macrophage elastase
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A182G
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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
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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
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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
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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
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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
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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
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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
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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
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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
E219A
I180S
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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
M103F
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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
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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
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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
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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
R117S
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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
additional information
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site-directed mutagenesis, inactive mutant, autolysis of the mutant is prevented
E219A
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NMR studies used MMP-12 preserved by E219A substitution of the general base
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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