MMP20

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Matrix metallopeptidase 20
Matrix metallopeptidase 20
according to PDB  2JSD
Properties of human protein
Mass / length primary structure 376 amino acids
Cofactor 2 Zn 2+ , Ca 2+
Identifier
Gene name MMP20
External IDs
Enzyme classification
EC, category 3.4.24. ,  Metalloprotease
MEROPS M10.019
Response type Proteolysis
Substrate Amelogenin, Aggregan, COMP
Occurrence
Homology family MMP
Parent taxon Eukaryotes
Orthologue
human mouse
Entrez 9313 30800
Ensemble ENSG00000137674 ENSMUSG00000018620
UniProt O60882 Q3LRH7
Refseq (mRNA) NM_004771 NM_013903
Refseq (protein) NP_004762 NP_038931
Gene locus Chr chr11: 101.95 - 102 Mb Chr chr9: 7.63 - 7.67 Mb
PubMed search 9313 30800

Matrix metallopeptidase 20 (enamelysin) , also known as MMP20 , is a peptidase that is found in all eukaryotes and breaks down the dental proteins amelogenin , aggrecan and COMP in humans. Mutations in the MMP20 gene can lead to amelogenesis imperfecta .

The proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of the extracellular matrix and exert their function in numerous physiological processes, such as in the context of embryonic development , reproduction, tissue remodeling but also in disease processes such as arthritis and tumor metastasis. Most MMPs are released from the cell as inactive protein precursors and activated by cleavage processes using extracellular proteinases. The protein described here degrades amelogenin, the main protein in the enamel matrix. It is therefore believed that it plays a role in the formation of tooth enamel . A mutation of the gene for MMP20, which disrupts the normal splicing of the MMP20 mRNA and leads to the translation being terminated prematurely, has been linked to a form of amelogenesis imperfecta . MMP20 belongs to a group of a gene cluster of different MMP genes on chromosome 11q 22.3.

literature

  • Nagase H, Woessner JF: Matrix metalloproteinases. in: J. Biol. Chem. vol. 274.31 pg. 21491-4 (1999) PMID 10419448
  • Bartlett JD, Simmer JP: Proteinases in developing dental enamel. in: Crit. Rev. Oral Biol. Med. Vol. 10.4 pg. 425-41 (2000) PMID 10634581
  • Pendás AM, Santamaría I, Alvarez MV, et al. : Fine physical mapping of the human matrix metalloproteinase genes clustered on chromosome 11q22.3. in: Genomics vol. 37.2 pg. 266-8 (1997) PMID 8921407
  • Llano E, Pendás AM, Knäuper V, et al. : Identification and structural and functional characterization of human enamelysin (MMP-20). in: Biochemistry vol. 36.49 pg. 15101-8 (1998) PMID 9398237
  • Stracke JO, Fosang AJ, Last K, et al. : Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP). in: FEBS Lett . vol. 478.1-2 pg. 52-6 (2000) PMID 10922468
  • Terp GE, Christensen IT, Jørgensen FS: Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes. in: J. Biomol. Struct. Dyn. Vol. 17.6 pg. 933-46 (2000) PMID 10949161
  • Väänänen A, Srinivas R, Parikka M, et al. : Expression and regulation of MMP-20 in human tongue carcinoma cells. in: J. Dent. Res. Vol. 80.10 pg. 1884-9 (2001) PMID 11706946
  • Väänänen A, Tjäderhane L, Eklund L, et al. : Expression of collagen XVIII and MMP-20 in developing teeth and odontogenic tumors. in: Matrix Biol. vol. 23.3 pg. 153-61 (2005) PMID 15296943
  • Kim JW, Simmer JP, Hart TC, et al. : MMP-20 mutation in autosomal recessive pigmented hypomaturation amelogenesis imperfecta. in: J. Med. Genet. vol. 42.3 pg. 271-5 (2006) PMID 15744043

Individual evidence

  1. ↑ a b Entrez Gene: MMP20 matrix metallopeptidase 20 (enamelysin) . Retrieved January 11, 2011.
  2. ↑ UniProt entry