Metalloproteinase requires zinc mineral to be present before degradation of collagen occurs.
An enzyme that can degrade proteins, including collagen, that are typically present in the gaps between cells in tissues (i.e., extracellular matrix proteins). These enzymes are referred to as metalloproteinases because they require calcium or zinc atoms to function effectively. Angiogenesis, tumor cell metastasis, and wound healing all require matrix metalloproteinases.
Of the four primary protease categories, metalloproteases are the most varied, with more than 50 families now recognized. A divalent cation, typically zinc, activates the water molecule in these enzymes. Three or more amino acid ligands are often used to hold the metal ion in place.
Thus from above conclusion we can say that the degradation of collagen and other ECM proteins is achieved through a family of metalloproteinases, which require zinc for their activity.
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