Leu- and -Tyr16Leu- in the B chain of insulin [2]
Reaction: Hydrolysis of soluble and insoluble elastin [1]. Specific cleavages are also produced at -Ala14Leu- and -Tyr16Leu- in the B chain of insulin [2]
Other names: metalloelastase; human macrophage metalloelastase (HME)
Comments: This enzyme is synthesized as a proenzyme of 53 kDa that is converted to an active form of 22 kDa. cDNA sequences have been obtained for the mouse [3] and human [4] enzymes. In peptidase family M10 (interstitial collagenase family)
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 9004-06-2
References:
1. Banda, M.J. and Werb, Z. Mouse macrophage elastase. Purification and characterization as a metalloproteinase. Biochem. J. 193 (1981) 589-605. [PMID: 7030312]
2. Kettner, C., Shaw, E., White, R. and Janoff, A. The specificity of macrophage elastase on the insulin B-chain. Biochem. J. 195 (1981) 369-372. [PMID: 7032505]
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. Molecular cloning, chromosomal localization, and bacterial expression of a murine macrophage metalloelastase. J. Biol. Chem. 267 (1992) 4664-4671. [PMID: 1537850]
4. Shapiro, S.D., Kobayashi, D.K. and Ley, T.J. Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages. J. Biol. Chem. 268 (1993) 23824-23829. [PMID: 8226919]