Skip to main content

MMP12

Domain

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Function

May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.

Sequence similarities

Belongs to the peptidase M10A family.

Tissue specificity

Found in alveolar macrophages but not in peripheral blood monocytes.

Cellular localization

  • Secreted
  • Extracellular space
  • Extracellular matrix

Alternative names

  • Macrophage metalloelastase
  • MME
  • Macrophage elastase
  • Matrix metalloproteinase-12
  • ME
  • hME
  • MMP-12
  • MMP12
  • HME

Target type

Proteins

Primary research area

Immuno-oncology

Molecular weight

54002Da