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Literature summary for 3.4.24.65 extracted from

  • Houghton, A.M.; Hartzell, W.O.; Robbins, C.S.; Gomis-Rueth, F.X.; Shapiro, S.D.
    Macrophage elastase kills bacteria within murine macrophages (2009), Nature, 460, 637-641.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information 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 Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
phagolysosome macrophage Mus musculus 32010
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus 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 ?
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?

Organism

Organism UniProt Comment Textmining
Mus musculus
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-
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Source Tissue

Source Tissue Comment Organism Textmining
macrophage MMP12 is an enzyme predominantly expressed in mature tissue macrophages Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 Mus musculus ?
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?

Subunits

Subunits Comment Organism
More the antimicrobial properties of MMP12 do not reside within its catalytic domain, but rather within the carboxy-terminal domain, which contains a unique four amino acid sequence on an exposed beta loop of the protein that is required for the observed antimicrobial activity, within the sequence designated SR-20, i.e. 344-SRNQLFLFKDEKYWLINNLV-363. Three-dimensional homology modeling of mouse MMP12 C-terminal domain, overview Mus musculus

Synonyms

Synonyms Comment Organism
matrix metalloproteinase 12
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Mus musculus
MMP12
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Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
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antimicrobial activity assay at Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
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antimicrobial activity assay at Mus musculus

General Information

General Information Comment Organism
physiological function 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. MMP12 is implicated in several disease processes, including emphysema Mus musculus