IED ID | IndEnz0002007809 |
Enzyme Type ID | protease007809 |
Protein Name |
Matrix metalloproteinase-20 MMP-20 EC 3.4.24.- Enamel metalloproteinase Enamelysin |
Gene Name | MMP20 |
Organism | Bos taurus (Bovine) |
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 Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
Enzyme Sequence | MLPASGLAVLLVTALKFSTAAPSLPAASPRTSRNNYRLAQAYLDKYYTKKGGPQIGEMVARGGNSTVKKIKELQEFFGLRVTGKLDRATMDVIKRPRCGVPDVANYRLFPGEPKWKKNTLTYRISKYTPSMTPAEVDRAMEMALRAWSSAVPLNFVRINAGEADIMISFETGDHGDSYPFDGPRGTLAHAFAPGEGLGGDTHFDNAEKWTMGTNGFNLFTVAAHEFGHALGLAHSTDPSALMFPTYKYQNPYGFRLPKDDVKGIQALYGPRRAFSGKPTAPHGPPHNPSIPDLCDSNLSFDAVTMLGKELLLFRDRIFWRRQVHLMSGIRPSTITSSFPQLMSNVDAAYEVAERGTAYFFKGPHYWITRGFQMQGPPRTIYDFGFPRYVQRIDAAVYLKDAQKTLFFVGDEYYSYDERKRKMEKDYPKSTEEEFSGVNGQIDAAVELNGYIYFFSGPKAYKSDTEKEDVVSELKSSSWIGC |
Enzyme Length | 481 |
Uniprot Accession Number | O18767 |
Absorption | |
Active Site | ACT_SITE 225; /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-Ser-|-Phe-361' site. {ECO:0000250|UniProtKB:O60882}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Disulfide bond (1); Glycosylation (2); Metal binding (21); Motif (1); Propeptide (1); Repeat (4); Sequence conflict (1); Signal peptide (1) |
Keywords | Autocatalytic cleavage;Calcium;Direct protein sequencing;Disulfide bond;Extracellular matrix;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. |
Modified Residue | |
Post Translational Modification | PTM: Autoactivates at least at the 105-Asn-|-Tyr-106 site. {ECO:0000250}. |
Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | MOTIF 96..103; /note=Cysteine switch; /evidence=ECO:0000250 |
Gene Encoded By | |
Mass | 53,781 |
Kinetics | |
Metal Binding | METAL 98; /note=Zinc 1; in inhibited form; /evidence=ECO:0000250; METAL 162; /note=Calcium 1; /evidence=ECO:0000250; METAL 163; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 164; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 174; /note=Zinc 2; /evidence=ECO:0000250; METAL 176; /note=Zinc 2; /evidence=ECO:0000250; METAL 181; /note=Calcium 2; /evidence=ECO:0000250; METAL 182; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 184; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 186; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 189; /note=Zinc 2; /evidence=ECO:0000250; METAL 195; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 196; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 198; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 200; /note=Calcium 1; /evidence=ECO:0000250; METAL 202; /note=Zinc 2; /evidence=ECO:0000250; METAL 204; /note=Calcium 2; /evidence=ECO:0000250; METAL 207; /note=Calcium 2; /evidence=ECO:0000250; METAL 224; /note=Zinc 1; catalytic; /evidence=ECO:0000250; METAL 228; /note=Zinc 1; catalytic; /evidence=ECO:0000250; METAL 234; /note=Zinc 1; catalytic; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda | 3.4.24.B6; |