Matrix metalloproteinases (MMPs) or matrixins may play a role in the degradation and remodeling of the extracellular matrix (ECM) during development or in response to stresses (PubMed:10574937). Can cleave myelin basic protein as well as fluorigenic peptide substrates, McaPLANvaDpaAR-NH(2) and McaPChaGNvaHADpa-NH(2) 4-fold more efficiently than McaPLGLDpaAR-NH(2) (QF24) (PubMed:10574937). Active on myelin basic protein (MBP) and, to some extent, on McaPLGLDpaAR-NH(2) (QF24) and beta-casein (PubMed:24156403). Binds 2 Zn(2+) ions per subunit. Inhibited by human TIMP-1 and TIMP-2 and by the peptide hydroxamate inhibitor (BB-94) (PubMed:10574937). Repressed by acetohydroxamic acid (AHA) (PubMed:24156403). Optimum pH is 7-8. Optimum temperature is 45-55 degrees Celsius. Mostly expressed in flowers, roots and stems, and, to a lower extent, in leaves. 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. Belongs to the peptidase M10A family. Matrix metalloproteinases (MMPs) subfamily.