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Literature summary for 3.4.24.65 extracted from

  • 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 (2007), J. Mol. Biol., 374, 1333-1344.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
E219A site-directed mutagenesis, inactive mutant, autolysis of the mutant is prevented Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
CGS-27023A a hydroxamate inhibitor Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens MMP-12 exacerbates atherosclerosis, emphysema, aortic aneurysm, rheumatoid arthritis, and inflammatory bowel disease ?
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?

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Source Tissue

Source Tissue Comment Organism Textmining
macrophage MMP-12 is secreted by macrophages at sites of inflammation Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information MMP-12 exacerbates atherosclerosis, emphysema, aortic aneurysm, rheumatoid arthritis, and inflammatory bowel disease Homo sapiens ?
-
?
additional information active site structure, surfaces and internal pocket between helix B and beta-strand IV in the active-site cleft, overview Homo sapiens ?
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?

Subunits

Subunits Comment Organism
More NMR structure determination and analysis of unprocessed enzyme mutant E219A in absence of inhibitor, comparison to the enzyme crystal structure, PDB code 1JK3, active site structure, overview Homo sapiens

Synonyms

Synonyms Comment Organism
human metalloelastase
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Homo sapiens
Macrophage elastase
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Homo sapiens
macrophage metalloelastase
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Homo sapiens
Matrix metalloproteinase-12
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Homo sapiens
MMP-12
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Homo sapiens