| IED ID | IndEnz0002006319 |
| Enzyme Type ID | protease006319 |
| Protein Name |
Matrix metalloproteinase-20 MMP-20 EC 3.4.24.- Enamel metalloproteinase Enamelysin |
| Gene Name | Mmp20 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MKVLPASGLAVLVTALKFATADPNLLAATPRTFRSNYHLAQAYLDKYYTKKGGPQAGEMVARESNPMIRRIKELQIFFGLKVTGKLDQNTMNVIKKPRCGVPDVANYRLFPGEPKWKKNILTYRISKYTPSMSPTEVDKAIQMALHAWSTAVPLNFVRINSGEADIMISFETGDHGDSYPFDGPRGTLAHAFAPGEGLGGDTHFDNAEKWTMGTNGFNLFTVAAHEFGHALGLGHSTDPSALMYPTYKYQNPYRFHLPKDDVKGIQALYGPRKIFPGKPTMPHIPPHKPSIPDLCDSSSSFDAVTMLGKELLFFKDRIFWRRQVHLPTGIRPSTITSSFPQLMSNVDAAYEVAERGIAFFFKGPHYWVTRGFHMQGPPRTIYDFGFPRHVQRIDAAVYLKEPQKTLFFVGEEYYSYDERKKKMEKDYPKNTEEEFSGVSGHIDAAVELNGYIYFFSGRKTFKYDTEKEDVVSVVKSSSWIGC |
| Enzyme Length | 482 |
| Uniprot Accession Number | P57748 |
| Absorption | |
| Active Site | ACT_SITE 226; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. Cleaves aggrecan at the '360-Asn-|-Phe-361' site. {ECO:0000250|UniProtKB:O60882}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Metal binding (21); Motif (1); Propeptide (1); Repeat (4); Signal peptide (1) |
| Keywords | Autocatalytic cleavage;Calcium;Disulfide bond;Extracellular matrix;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Autoactivates at least at the 106-Asn-|-Tyr-107 site. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10932192; 10949577; 11023266; 12206593; 12393861; 15063736; 15296943; 15525533; 15557396; 15734845; 15748894; 16113801; 16674657; 16674658; 16998127; 17364666; 18714142; 20147630; 20487000; 20665536; 21144496; 21267068; 21285247; 21386097; 21454549; 21525715; 22243238; 22243247; 22243248; 22351765; 22866057; 23421805; 24067343; 24072097; 24466234; 26513418; 27066511; 27403713; 28174279; 29535349; 29684584; 30149392; 30929801; 32674056; 33659251; 34012043; |
| Motif | MOTIF 97..104; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 54,373 |
| Kinetics | |
| Metal Binding | METAL 99; /note=Zinc 1; in inhibited form; /evidence=ECO:0000250; METAL 163; /note=Calcium 1; /evidence=ECO:0000250; METAL 164; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 165; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 175; /note=Zinc 2; /evidence=ECO:0000250; METAL 177; /note=Zinc 2; /evidence=ECO:0000250; METAL 182; /note=Calcium 2; /evidence=ECO:0000250; METAL 183; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 185; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 187; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 190; /note=Zinc 2; /evidence=ECO:0000250; METAL 196; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 197; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 199; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 201; /note=Calcium 1; /evidence=ECO:0000250; METAL 203; /note=Zinc 2; /evidence=ECO:0000250; METAL 205; /note=Calcium 2; /evidence=ECO:0000250; METAL 208; /note=Calcium 2; /evidence=ECO:0000250; METAL 225; /note=Zinc 1; catalytic; /evidence=ECO:0000250; METAL 229; /note=Zinc 1; catalytic; /evidence=ECO:0000250; METAL 235; /note=Zinc 1; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B6; |