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Gene Review

MMP20  -  matrix metallopeptidase 20

Homo sapiens

Synonyms: AI2A2, Enamel metalloproteinase, Enamelysin, MMP-20, Matrix metalloproteinase-20
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Disease relevance of MMP20


High impact information on MMP20

  • MMP-2 and MMP-20 were purified from over 150 g of porcine dentin powder and incubated with DSP-DGP and DPP [4].
  • In healthy tissues, MMP-20 is observed in the enamel organ and pulp organ of developing teeth and is present only as an activated enzyme [5].
  • Since type V collagen is not present in dental enamel but is an otherwise widely distributed collagen, and since only active MMP-20 has been observed in teeth, our data suggest that control of MMP-20 activity is primarily regulated by transcriptional means [5].
  • We asked if the highly restricted MMP-20 expression pattern was associated with a broad substrate specificity that might preclude its expression in other tissues [5].
  • Among the non-tooth tissues assayed, MMP-20 transcripts were identified only in minute quantities within the large intestine [5].

Biological context of MMP20


Anatomical context of MMP20


Associations of MMP20 with chemical compounds


Enzymatic interactions of MMP20

  • Furthermore, recombinant porcine enamelysin was demonstrated to cleave recombinant porcine amelogenin at virtually all of the sites that have previously been described in vivo [12].
  • Enamelysin cleaved the 32-kDa enamelin only after it was deglycosylated [13].
  • We tested the hypothesis that MMP-20 is the protease that cleaves AMBN [14].

Other interactions of MMP20

  • To determine the frequency of mutations in these genes, we analyzed 15 Turkish probands with autosomal-recessive hypomaturation AI for MMP20 and KLK4 gene mutations [6].
  • Matrix metalloproteinase (MMP)-19 and MMP-20 (enamelysin) are two recently discovered members of the MMP family [7].
  • Enamelysin (MMP-20) is the foremost enamel matrix-processing enzyme [8].
  • Human enamelysin (MMP-20) has a domain organization similar to other MMPs, including a signal peptide, a prodomain with the conserved motif PRCGVPD involved in maintaining enzyme latency, a catalytic domain with a Zn-binding site, and a COOH-terminal fragment similar to the sequence of hemopexin [2].
  • How do enamelysin and kallikrein 4 process the 32-kDa enamelin [13]?

Analytical, diagnostic and therapeutic context of MMP20


  1. Expression of collagen XVIII and MMP-20 in developing teeth and odontogenic tumors. Väänänen, A., Tjäderhane, L., Eklund, L., Heljasvaara, R., Pihlajaniemi, T., Herva, R., Ding, Y., Bartlett, J.D., Salo, T. Matrix Biol. (2004) [Pubmed]
  2. Identification and structural and functional characterization of human enamelysin (MMP-20). Llano, E., Pendás, A.M., Knäuper, V., Sorsa, T., Salo, T., Salido, E., Murphy, G., Simmer, J.P., Bartlett, J.D., López-Otín, C. Biochemistry (1997) [Pubmed]
  3. Immunohistochemical detection and distribution of enamelysin (MMP-20) in human odontogenic tumors. Takata, T., Zhao, M., Uchida, T., Wang, T., Aoki, T., Bartlett, J.D., Nikai, H. J. Dent. Res. (2000) [Pubmed]
  4. Dentin Sialophosphoprotein Is Processed by MMP-2 and MMP-20 in Vitro and in Vivo. Yamakoshi, Y., Hu, J.C., Iwata, T., Kobayashi, K., Fukae, M., Simmer, J.P. J. Biol. Chem. (2006) [Pubmed]
  5. MMP-20 is predominately a tooth-specific enzyme with a deep catalytic pocket that hydrolyzes type V collagen. Turk, B.E., Lee, D.H., Yamakoshi, Y., Klingenhoff, A., Reichenberger, E., Wright, J.T., Simmer, J.P., Komisarof, J.A., Cantley, L.C., Bartlett, J.D. Biochemistry (2006) [Pubmed]
  6. MMP20 active-site mutation in hypomaturation amelogenesis imperfecta. Ozdemir, D., Hart, P.S., Ryu, O.H., Choi, S.J., Ozdemir-Karatas, M., Firatli, E., Piesco, N., Hart, T.C. J. Dent. Res. (2005) [Pubmed]
  7. Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP). Stracke, J.O., Fosang, A.J., Last, K., Mercuri, F.A., Pendás, A.M., Llano, E., Perris, R., Di Cesare, P.E., Murphy, G., Knäuper, V. FEBS Lett. (2000) [Pubmed]
  8. Expression, structure, and function of enamel proteinases. Simmer, J.P., Hu, J.C. Connect. Tissue Res. (2002) [Pubmed]
  9. Fluoride down-regulates the expression of matrix metalloproteinase-20 in human fetal tooth ameloblast-lineage cells in vitro. Zhang, Y., Yan, Q., Li, W., Denbesten, P.K. Eur. J. Oral Sci. (2006) [Pubmed]
  10. Role of matrix proteases in processing enamel proteins. Woessner, J.F. Connect. Tissue Res. (1998) [Pubmed]
  11. X-linked amelogenesis imperfecta may result from decreased formation of tyrosine rich amelogenin peptide (TRAP). Li, W., Gao, C., Yan, Y., DenBesten, P. Arch. Oral Biol. (2003) [Pubmed]
  12. Proteinases in developing dental enamel. Bartlett, J.D., Simmer, J.P. Crit. Rev. Oral Biol. Med. (1999) [Pubmed]
  13. How do enamelysin and kallikrein 4 process the 32-kDa enamelin? Yamakoshi, Y., Hu, J.C., Fukae, M., Yamakoshi, F., Simmer, J.P. Eur. J. Oral Sci. (2006) [Pubmed]
  14. Processing of Ameloblastin by MMP-20. Iwata, T., Yamakoshi, Y., Hu, J.C., Ishikawa, I., Bartlett, J.D., Krebsbach, P.H., Simmer, J.P. J. Dent. Res. (2007) [Pubmed]
  15. One-step sandwich enzyme immunoassay using monoclonal antibodies for detection of human enamelysin (MMP-20). Wang, T., Aoki, T., Iwata, K., Takata, T., Uchida, T., Knäuper, V., Llano, E., Okada, Y., Bartlett, J.D. Eur. J. Oral Sci. (2000) [Pubmed]
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