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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | The MEROPS peptidase family M10, subfamily M10A, consists of extracellular metalloproteases, such as collagenase and stromelysin, that degrade the extracellular matrix and are known as matrixins or matrix metalloproteinases (MMPs). They are zinc-dependent, calcium-activated proteases synthesised as inactive precursors(zymogens), which are proteolytically cleaved to yield the active enzyme [ , ].All matrixins and related proteins possess two domains: an N-terminal domain, and a zinc-binding active site domain. The N-terminal domain peptide, cleaved during the activation step, includes a conserved PRCGVPDV octapeptide, known as the cysteine switch, whose Cys residue chelates the active site zinc atom, rendering the enzyme inactive [ , ]. The active enzyme degrades components of the extracellular matrix, playing a role in the initial steps of tissue remodelling during morphogenesis, wound healing, angiogenesis and tumour invasion [, ]. Although it was initially thought that the primary function of these enzymes is to degrade proteins of the extracellular matrix, MMPs have a much broader spectrum of activity that includes the proteolytic processing of cytokines, growth factors, growth factor receptors, and cell adhesion molecules [, ]. | Name | Peptidase M10A |
| Short Name | Pept_M10A | Type | Family |
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