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Literature summary for 3.4.24.B6 extracted from

  • Chun, Y.H.; Yamakoshi, Y.; Yamakoshi, F.; Fukae, M.; Hu, J.C.; Bartlett, J.D.; Simmer, J.P.
    Cleavage site specificity of MMP-20 for secretory-stage ameloblastin (2010), J. Dent. Res., 89, 785-790.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.B6

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged MMP-20 Sus scrofa

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Sus scrofa
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ameloblastin + H2O Sus scrofa N-terminal ameloblastin cleavage products of 13, 15, and 17 kDa accumulate in the sheath space throughout the enamel layer ameloblastin fragments
-
 ?
amelogenin + H2O Sus scrofa
-
 amelogenin fragments
-
 ?
enamelin + H2O Sus scrofa
-
 enamelin fragments
-
 ?

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged MMP-20 by metal affinity chromatography Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
ameloblast
-
 Sus scrofa
-
enamel layer Enamel formation progresses through a secretory and a maturation stage, MMP-20 is expressed during the secretory and early-maturation stages Sus scrofa
-
tooth
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ameloblastin + H2O N-terminal ameloblastin cleavage products of 13, 15, and 17 kDa accumulate in the sheath space throughout the enamel layer Sus scrofa ameloblastin fragments
-
 ?
ameloblastin + H2O MMP-20 cleaves the recombinant porcine substrate at multiple sites on the N-terminal side of the protein to fragments that show smaller bands of 7-25 kDa and larger products of 45-65 kDa. MMP-20 starts the cleavage on the N-terminal side of the protein, so that the N-terminal cleavage products are smaller than the C-terminal cleavage products digested by MMP-20 initially at one of three sites—after Gln130. The substrate is digested by MMP-20 initially at one of three sites, after Gln130, Arg170, and Ala222, generating 6 cleavage products. These initial products are then cleaved a second or third time at these same sites, as well as at secondary sites that are located mostly near the C-terminus, after Gly300, Arg319, Ala342, and Asn31 Arg170, and Ala222, generating 6 cleavage products. These initial products are then cleaved a second or third time at these same sites, as well as at secondary sites that are located mostly near the C-terminus, after Gly300, Arg319, Ala342, and Asn31 Sus scrofa ameloblastin fragments mass spectrometry product analysis, overview ?
amelogenin + H2O
-
 Sus scrofa amelogenin fragments
-
 ?
casein + H2O zymography Sus scrofa ?
-
 ?
enamelin + H2O
-
 Sus scrofa enamelin fragments
-
 ?

Synonyms

Synonyms Comment Organism
enamelysin
-
 Sus scrofa
matrix metalloproteinase 20
-
 Sus scrofa
MMP-20
-
 Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Sus scrofa

General Information

General Information Comment Organism
physiological function dental enamel is the product of ameloblasts and requires the secretion of the three matrix proteins amelogenin, ameloblastin, and enamelin, which are hydrolyzed by MMP-20 and kallikrein 4 and removed from the matrix. Enamel formation progresses through a secretory and a maturation stage, MMP-20 is expressed during the secretory and early-maturation stages Sus scrofa