Metalloprotease
A metalloprotease, also termed a metalloproteinase, is an enzyme that catalyzes the hydrolysis of peptide bonds in proteins, relying on metal ions—most commonly zinc (Zn²⁺), but also calcium (Ca²⁺), manganese (Mn²⁺), or cobalt (Co²⁺)—as essential cofactors for its catalytic activity. Classified within the broader group of proteases (peptidases), metalloproteases are distinct due to their metal-ion […]
Microbiome Signatures identifies and validates condition-specific microbiome shifts and interventions to accelerate clinical translation. Our multidisciplinary team supports clinicians, researchers, and innovators in turning microbiome science into actionable medicine.
Karen Pendergrass
A metalloprotease, also termed a metalloproteinase, is an enzyme that catalyzes the hydrolysis of peptide bonds in proteins, relying on metal ions—most commonly zinc (Zn²⁺), but also calcium (Ca²⁺), manganese (Mn²⁺), or cobalt (Co²⁺)—as essential cofactors for its catalytic activity. Classified within the broader group of proteases (peptidases), metalloproteases are distinct due to their metal-ion dependence, contrasting with other proteases that employ serine or cysteine residues for catalysis. Many feature a conserved metal-binding motif, such as the HEXXH sequence in matrix metalloproteases (MMPs), where the metal ion coordinates with amino acid residues to stabilize the enzyme-substrate complex and enable peptide bond cleavage. These enzymes are vital in processes like extracellular matrix remodeling, cell signaling, protein degradation, and microbial virulence, playing significant roles in both physiological events (e.g., wound healing) and pathological conditions (e.g., inflammation, cancer metastasis, and neurodegenerative diseases).