Metallopeptidase

Metallopeptidases (also called metalloproteinases or metalloproteases) are a broad class of **protease enzymes** whose **catalytic mechanism requires a metal ion**, most commonly zinc[1]. They function mainly by cleaving peptide bonds in proteins, with subclasses that act as exopeptidases or endopeptidases. Their activity can be abolished by chelating agents that disrupt the metal binding[1]. Metallopeptidases are divided into numerous families based on sequence and structure, with notable members including **matrix metalloproteinases (MMPs)**, ADAMs, and others[4][5][6]. They are essential in degrading extracellular matrix components, regulating tissue remodeling, cell signaling, and immune responses, but aberrant activity is associated with diseases such as cancer, inflammation, and degenerative conditions[4]. The name "metallopeptidase" is a general class, not a single specific target—therefore, further specificity (such as "matrix metallopeptidase 9") is needed for clear therapeutic targeting. Caveats: - "Metallopeptidase" refers to a vast **enzyme class or family**, not a specific molecular target, so the entry is too generic for most drug development purposes[1][3][4]. - It is advisable to specify particular metallopeptidase(s) for structured database mapping or therapeutic investigation.

Other names

MetalloproteinaseMetalloprotease

Inhibition of Zn²⁺-dependent catalytic activity (chelating the essential metal ion); Blockade of substrate binding or active site configuration