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
-
alveolar
- elastin
- fibrosis
-
smoke
- airway
- timp-1
-
cigarette
-
lavage
-
bronchoalveolar
- endothelial
- metastasis
- aortic
- tnf
- artery
- chemokine
- monocyte
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smoking
- plaque
- aneurysm
- angiogenesis
- atherosclerotic
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zymography
-
smoke-induced
-
elastolytic
- proteinases
- plasminogen
- asthma
-
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
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Crystallization
Crystallization on EC 3.4.24.65 - macrophage elastase
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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
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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
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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