3.4.24.B6: matrix metalloproteinase-20
This is an abbreviated version!
For detailed information about matrix metalloproteinase-20, go to the full flat file.
Word Map on EC 3.4.24.B6
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3.4.24.B6
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amelogenins
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amelogenesis
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tooth
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klk4
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dentin
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imperfecta
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odontoblasts
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ameloblastin
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enamelin
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amelx
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incisor
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sialophosphoprotein
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hypomineralized
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odontogenic
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apatite
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maturation-stage
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fluorosis
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tooth-specific
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fam83h
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kallikrein-4
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kallikrein-related
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hypomaturation
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secretory-stage
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tuftelin
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dentinogenesis
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odontogenesis
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ameloblast-like
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dentin-pulp
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decussating
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dentino-enamel
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tyrosine-rich
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crystallite
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pharmacology
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medicine
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degradation
- 3.4.24.B6
- amelogenins
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amelogenesis
- tooth
- klk4
- dentin
- imperfecta
- odontoblasts
- ameloblastin
- enamelin
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amelx
- incisor
- sialophosphoprotein
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hypomineralized
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odontogenic
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apatite
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maturation-stage
- fluorosis
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tooth-specific
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fam83h
- kallikrein-4
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kallikrein-related
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hypomaturation
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secretory-stage
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tuftelin
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dentinogenesis
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odontogenesis
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ameloblast-like
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dentin-pulp
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decussating
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dentino-enamel
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tyrosine-rich
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crystallite
- pharmacology
- medicine
- degradation
Reaction
proteolytic cleavage of ameloblastin =
Synonyms
enamel metalloproteinase, enamel protease, enamelysin, M10.019, matrix metalloproteinase 20, MMP-20, MMP20
ECTree
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Substrates Products
Substrates Products on EC 3.4.24.B6 - matrix metalloproteinase-20
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REACTION DIAGRAM
amelogenin + H2O
23 kDa amelogenin + 5 kDa tyrosine-rich amelogenin peptide
cleaves amelogenin between Trp45 and Leu46
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amelogenin + H2O
amelogenin fragments rH163 + rH146
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in high phosphates conditions (20.9 mM KH2PO4) no cleavage site is observed in the central region of residues Q54P146, which also shows the slowest cleavage rate with the maximum accumulation of fragment rH163 at 4 h time-point. In the no calcium and phosphates conditions, the accumulation of rH163 reaches the maximum amount at 1 h and the cleavage in the central region Q54-P146 appears only after 5 h. Under high calcium conditions (33.4 mM CaCl2), the fastest cleavage rate is observed and also few exclusive and additional cleavage sites at T61, H67. Other conditions also show some exclusive cleavage sites such as P2 for no calcium and phosphates, P50 for low calcium and phosphates and G10 for high calcium and phosphates. The N-terminal positions Y11, N13, F14, S15, E17, K23, W24, P33, G42, and S53 and the C-terminal positions P155 and T158 are cleaved in all conditions used
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amylogenin + H2O
4 major peptide fragments of MWs 24 kDa, 23 kDa, 22 kDa, and 20 kDa
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cartilage oligomeric matrix protein + H2O
60 kDa protein
100 kDa protein substrate
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dentin sialophosphoprotein + H2O
dentin sialoprotein-glycoprotein + dentin phosphoprotein
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dentin sialoprotein-glycoprotein + H2O
dentin sialoprotein + dentin glycoprotein
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enamel protein + H2O
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MMP-20 is secreted along with enamel proteins by secretory stage ameloblasts into the enamel matrix of developing teeth. Enamel protein cleavage products accumulate in the space between the crystal ribbons, helping to support them. MMP-20 steadily cleaves accumulated enamel proteins, so their concentration decreases with depth. The principle functions of MMP-20 in dental enamel formation is to facilitate the orderly replacement of organic matrix with mineral, generating an enamel layer that is harder, less porous, and unstained by retained enamel proteins
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endostatin + H2O
peptides
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comparison of efficiency to several other proteinases
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leucine-rich amylogenin peptide + H2O
leucine-rich amylogenin residues 181-186 + leucine-rich amylogenin residues 187-188
corresponds to residues 181-188 of amylogenin, recombinant enzyme, cleavage site is P186-A187
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Mca-PLA-norvaline-Dpa-AR-NH2 + H2O
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synthetic fluorogenic substrate
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tyrosine-rich amylogenin peptide + H2O
tyrosine-rich amylogenin residues 36-45 + tyrosine-rich amylogenin residues 46-49
corresponds to residues 36-49 of amylogenin, recombinant enzyme, cleavage site is W45-L46
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MMP-20 processes ameloblastin during the secretory stage of amelogenesis, cleaves glycosylated recombinant porcine ameloblastin after Pro2, Gln130, Gln139, Arg170, and Ala222. MMP-20 generates the 23-kDa ameloblastin starting at Tyr223, as well as the 17-kDa (Val1-Arg170) and 15-kDa (Val1-Gln130) ameloblastin cleavage products that concentrate in the sheath space during the secretory stage
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ameloblastin + H2O
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cleaves glycosylated recombinant porcine ameloblastin after Pro2, Gln130, Gln139, Arg170, and Ala222. MMP-20 generates the 23-kDa ameloblastin starting at Tyr223, as well as the 17-kDa (Val1-Arg170) and 15-kDa (Val1-Gln130) ameloblastin cleavage products that concentrate in the sheath space during the secretory stage
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ameloblastin fragments
MMP-20 cleaves ameloblastin after Pro2, Gln130, Gln139, Arg170, and Ala222
fragments of 23 kDa, 17 kDa, and 15 kDa
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ameloblastin + H2O
ameloblastin fragments
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N-terminal ameloblastin cleavage products of 13, 15, and 17 kDa accumulate in the sheath space throughout the enamel layer
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ameloblastin + H2O
ameloblastin fragments
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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 sitesafter 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
mass spectrometry product analysis, overview
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amelogenin + H2O
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cleavage loci: FSY/EVL, GGW/LHH, MFP/MQP, MLP/DLT, LTL/EAW, AWP/STD
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amelogenin + H2O
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amelogenin with a proline 41 to threonine mutation is hydrolyzed at a lower rate by matrix metalloproteinase 20 (MMP20), resulting in an inherited tooth enamel defect, amelogenesis
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amelogenin + H2O
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amelogenin with a proline 41 to threonine mutation is hydrolyzed at a lower rate by matrix metalloproteinase 20 (MMP20), resulting in an inherited tooth enamel defect, amelogenesis imperfecta. P41T mutation reduces the interactions between amelogenin and MMP20, leading to decreased degradation of amelogenin by MMP20, and resulting in amelogenesis imperfecta
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amelogenin + H2O
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cleavage loci: FSY/EVL, GGW/LHH, MFP/MQP, MLP/DLT, DLT/LEA, LTL/EAW, AWP/STD
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amelogenin + H2O
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MMP-20 is involved in amelogenin processing and degradation
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amelogenin + H2O
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amelogenin constitutes more than 90% of enamel extracellular matrix proteins in secretory-stage enamel
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amelogenin + H2O
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most of the secreted substrate is cleaved after Ser148 to generate the 20000 Da amelogenin (Met1-Ser148), which in turn is cleaved after Trp45 to yield the tyrosine-rich amelogenin polypeptide (Met1-Trp45) and the 13000 Da amelogenin (Leu46-Ser148)
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amelogenin + H2O
amelogenin fragments
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Mmp-20 cleaves amelogenin sequences after Pro162, Ser148, His62, Ala63, and Trp45. These cleavages generate all of the major cleavage products from tyrosine-rich amelogenin polypeptide that accumulate in porcine secretory stage enamel, i.e. the 23 kDa, 20 kDa, 13 kDa, 11 kDa, and 6 kDa amelogenins. And Mmp-20 cleaves leucine rich-amelogenin protein after Pro45 and Pro40, producing the two LRAP products, Mmp-20 cleavage site preferences, overview
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amylogenin + H2O
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recombinant substrate from pig or mouse, cleavage site determination by mass spectrometry, overview
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additional information
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multiple cleavages near the C-terminus
release of N-terminal dentin sialoprotein cleavage products ranging from 25-39 kDa
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additional information
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MMP-20 becomes functionally active when proteolytic cleavage removes the pro-domain to expose the zinc atom and free the active site for the enzyme to interact with its substrate
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additional information
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MMP-20 becomes functionally active when proteolytic cleavage removes the pro-domain to expose the zinc atom and free the active site for the enzyme to interact with its substrate
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additional information
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degradation of various components of the extracellular matrix during tooth development and pathological conditions
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additional information
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degradation of various components of the extracellular matrix during tooth development and pathological conditions
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additional information
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MMP-20 becomes functionally active when proteolytic cleavage removes the pro-domain to expose the zinc atom and free the active site for the enzyme to interact with its substrate
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additional information
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MMP-20 becomes functionally active when proteolytic cleavage removes the pro-domain to expose the zinc atom and free the active site for the enzyme to interact with its substrate
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additional information
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digestion of FRET-amelogenin peptides, labeled with 2-aminobenzoyl and 2,4-dinitrophenyl, by Mmp-20, overview
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additional information
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recombinant Mmp-20 is self-activated by its incubation in 4-aminophenylmercuric acetate in 10 mM CaCl2 for 24 h
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additional information
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in vitro, the formation of well-aligned bundles of enamel-like hydroxyapatite crystals is promoted in the presence of amelogenin (P173) with added MMP20, while only amorphous calcium phosphate particles are seen in the absence of MMP20. Fragment P148 has a somewhat lower capacity to stabilize amorphous calcium phosphate and prevents hydroxyapatite formation compared with P173 in the absence of MMP20, and essentially no hydroxyapatite formation is observed in the presence of somewhat higher concentrations of P148 regardless of MMP20 addition. MMP20 does not cleave fragment P148
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additional information
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in vitro, the formation of well-aligned bundles of enamel-like hydroxyapatite crystals is promoted in the presence of amelogenin (P173) with added MMP20, while only amorphous calcium phosphate particles are seen in the absence of MMP20. Fragment P148 has a somewhat lower capacity to stabilize amorphous calcium phosphate and prevents hydroxyapatite formation compared with P173 in the absence of MMP20, and essentially no hydroxyapatite formation is observed in the presence of somewhat higher concentrations of P148 regardless of MMP20 addition. MMP20 does not cleave fragment P148
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