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Macrophage elastase

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Macrophage elastase
Identifiers
EC no.3.4.24.65
CAS no.2594837
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Macrophage elastase (EC 3.4.24.65, metalloelastase, human macrophage metalloelastase (HME)) 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.

References

  1. ^ Banda, M.J. and Werb, Z. (1981). "Mouse macrophage elastase. Purification and characterization as a metalloproteinase". Biochem. J. 193: 589–605. PMID 7030312.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  2. ^ Kettner, C., Shaw, E., White, R. and Janoff, A. (1981). "The specificity of macrophage elastase on the insulin B-chain". Biochem. J. 195: 369–372. PMID 7032505.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  3. ^ Shapiro, S.D., Griffin, G.L., Gilbert, D.J., Jenkins, N.A., Copeland, N.G., Welgus, H.G., Senior, R.M. and Ley, T.J. (1992). "Molecular cloning, chromosomal localization, and bacterial expression of a murine macrophage metalloelastase". J. Biol. Chem. 267: 4664–4671. PMID 1537850.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  4. ^ Shapiro, S.D., Kobayashi, D.K. and Ley, T.J. (1993). "Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages". J. Biol. Chem. 268: 23824–23829. PMID 8226919.{{cite journal}}: CS1 maint: multiple names: authors list (link)

See also