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Macrophage elastase (EC 3.4.24.65, metalloelastase, human macrophage metalloelastase (HME), MMP-12) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction

Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at -Ala14-Leu- and -Tyr16-Leu- in the B chain of insulin

This enzyme belongs to the peptidase family M10.

See also

References

  1. ^ Banda MJ, Werb Z (February 1981). "Mouse macrophage elastase. Purification and characterization as a metalloproteinase". The Biochemical Journal. 193 (2): 589–605. PMID 7030312.
  2. ^ Kettner C, Shaw E, White R, Janoff A (May 1981). "The specificity of macrophage elastase on the insulin B-chain". The Biochemical Journal. 195 (2): 369–72. PMID 7032505.
  3. ^ Shapiro SD, Griffin GL, Gilbert DJ, Jenkins NA, Copeland NG, Welgus HG, Senior RM, Ley TJ (March 1992). "Molecular cloning, chromosomal localization, and bacterial expression of a murine macrophage metalloelastase". The Journal of Biological Chemistry. 267 (7): 4664–71. PMID 1537850.
  4. ^ Shapiro SD, Kobayashi DK, Ley TJ (November 1993). "Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages". The Journal of Biological Chemistry. 268 (32): 23824–9. PMID 8226919.

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