Macrophage elastase

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
Macrophage elastase
Identifiers
EC number3.4.24.65
CAS number2594837
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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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