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Matrilysin also known as matrix metalloproteinase-7 (MMP-7), pump-1 protease (PUMP-1), or uterine metalloproteinase is an enzyme in humans that is encoded by the MMP7 gene. [5] The enzyme ( EC 3.4.24.23 ) has also been known as matrin , putative (or punctuated) metalloproteinase-1 , matrix metalloproteinase pump 1 , PUMP-1 proteinase , PUMP ...
72 kDa type IV collagenase also known as matrix metalloproteinase-2 (MMP-2) and gelatinase A is an enzyme that in humans is encoded by the MMP2 gene. [5] The MMP2 gene is located on chromosome 16 at position 12.2.
Matrix metalloproteinases (MMPs), also known as matrix metallopeptidases or matrixins, are metalloproteinases that are calcium-dependent zinc-containing endopeptidases; [1] other family members are adamalysins, serralysins, and astacins. The MMPs belong to a larger family of proteases known as the metzincin superfamily. [2]
[2] Overall, all MMPs are inhibited by TIMPs once they are activated, but the gelatinases ( MMP-2 and MMP-9 ) can form complexes with TIMPs when the enzymes are in their latent form. The complex of latent MMP-2 (pro-MMP-2)with TIMP-2 serves to facilitate the activation of pro-MMP-2 at the cell surface by MT1-MMP ( MMP-14 ), a membrane-anchored MMP.
7077 21858 Ensembl ENSG00000035862 ENSMUSG00000017466 UniProt P16035 P25785 RefSeq (mRNA) NM_003255 NM_011594 RefSeq (protein) NP_003246 n/a Location (UCSC) Chr 17: 78.85 – 78.93 Mb Chr 11: 118.19 – 118.25 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Tissue inhibitor of metalloproteinases 2 (TIMP2) is a gene and a corresponding protein. The gene is a member of the TIMP gene ...
Metalloproteinase inhibitors are found in numerous marine organisms, including fish, cephalopods, mollusks, algae and bacteria. [5] Members of the M50 metallopeptidase family include: mammalian sterol-regulatory element binding protein (SREBP) site 2 protease and Escherichia coli protease EcfE, stage IV sporulation protein FB.
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The MMP family is formed by twenty related zinc-dependent enzymes. They are noted for having the ability to degrade extracellular matrix proteins, such as collagens , laminin , and proteoglycans . These calcium- and zinc-dependent proteases are activated at neutral pH and twenty-three have been found present in mammalian cells.