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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]
Stromelysin-1 also known as matrix metalloproteinase-3 (MMP-3) is an enzyme that in humans is encoded by the MMP3 gene. The MMP3 gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [ 5 ]
There are two subgroups of metalloproteinases: Exopeptidases, metalloexopeptidases (EC number: 3.4.17).; Endopeptidases, metalloendopeptidases (3.4.24). Well known metalloendopeptidases include ADAM proteins and matrix metalloproteinases, and M16 metalloproteinases such as Insulin Degrading Enzyme and Presequence Protease [1] [2]
216766 Ensembl ENSG00000082516 ENSMUSG00000037275 UniProt Q8TEQ6 Q8BX17 RefSeq (mRNA) NM_015465 NM_001252156 NM_001166669 NM_001166670 NM_001166671 NM_172558 NM_001374702 RefSeq (protein) NP_001239085 NP_056280 NP_001160141 NP_001160142 NP_001160143 NP_766146 NP_001361631 Location (UCSC) Chr 5: 154.89 – 154.94 Mb Chr 11: 58.01 – 58.06 Mb PubMed search Wikidata View/Edit Human View/Edit ...
The human MMP-20 gene contains 10 exons and is part of a cluster of matrix metalloproteinase genes that localize to human chromosome 11q22.3. [6] A mutation in this gene, which alters the normal splice pattern and results in premature termination of the encoded protein, has been associated with amelogenesis imperfecta. Enamel in the absence of ...
[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.
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