| IED ID | IndEnz0002006096 |
| Enzyme Type ID | protease006096 |
| Protein Name |
Macrophage metalloelastase MME EC 3.4.24.65 Macrophage elastase ME hME Matrix metalloproteinase-12 MMP-12 |
| Gene Name | MMP12 HME |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MKFLLILLLQATASGALPLNSSTSLEKNNVLFGERYLEKFYGLEINKLPVTKMKYSGNLMKEKIQEMQHFLGLKVTGQLDTSTLEMMHAPRCGVPDVHHFREMPGGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYGDPKENQRLPNPDNSEPALCDPNLSFDAVTTVGNKIFFFKDRFFWLKVSERPKTSVNLISSLWPTLPSGIEAAYEIEARNQVFLFKDDKYWLISNLRPEPNYPKSIHSFGFPNFVKKIDAAVFNPRFYRTYFFVDNQYWRYDERRQMMDPGYPKLITKNFQGIGPKIDAVFYSKNKYYYFFQGSNQFEYDFLLQRITKTLKSNSWFGC |
| Enzyme Length | 470 |
| Uniprot Accession Number | P39900 |
| Absorption | |
| Active Site | ACT_SITE 219 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in the B chain of insulin.; EC=3.4.24.65; |
| DNA Binding | |
| EC Number | 3.4.24.65 |
| Enzyme Function | FUNCTION: May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (33); Chain (1); Disulfide bond (1); Glycosylation (2); Helix (7); Metal binding (25); Motif (1); Natural variant (2); Propeptide (1); Repeat (4); Signal peptide (1); Turn (9) |
| Keywords | 3D-structure;Calcium;Disulfide bond;Extracellular matrix;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | INDUCTION: By exposure to bacterial lipopolysaccharides (LPS). Inhibited by dexamethasone. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000305 |
| Structure 3D | NMR spectroscopy (11); X-ray crystallography (73) |
| Cross Reference PDB | 1JIZ; 1JK3; 1OS2; 1OS9; 1RMZ; 1ROS; 1UTT; 1UTZ; 1Y93; 1YCM; 1Z3J; 2HU6; 2JXY; 2K2G; 2K9C; 2KRJ; 2MLR; 2MLS; 2N8R; 2OXU; 2OXW; 2OXZ; 2POJ; 2W0D; 2WO8; 2WO9; 2WOA; 2Z2D; 3BA0; 3EHX; 3EHY; 3F15; 3F16; 3F17; 3F18; 3F19; 3F1A; 3LIK; 3LIL; 3LIR; 3LJG; 3LK8; 3LKA; 3N2U; 3N2V; 3NX7; 3RTS; 3RTT; 3TS4; 3TSK; 3UVC; 4EFS; 4GQL; 4GR0; 4GR3; 4GR8; 4GUY; 4H30; 4H49; 4H76; 4H84; 4I03; 4IJO; 5CXA; 5CZM; 5D2B; 5D3C; 5I0L; 5I2Z; 5I3M; 5I43; 5I4O; 5L79; 5L7F; 5LAB; 5N5J; 5N5K; 6EKN; 6ELA; 6ENM; 6EOX; 6RD0; 6RLY; 7OVY; |
| Mapped Pubmed ID | 10187779; 10229672; 10386589; 10551873; 10807873; 10809722; 11119712; 11546917; 11577169; 11875051; 12032297; 12103254; 12195704; 12684035; 12742660; 12813751; 12858542; 1326552; 15080939; 15289103; 15474460; 15611040; 15654955; 15709175; 15723202; 15781250; 15802269; 15803400; 15809432; 15837315; 15868410; 15944607; 15950618; 15983040; 15987457; 15989693; 16082623; 16166618; 16311244; 16359550; 16481329; 1649600; 16676616; 16825321; 16855860; 16899369; 16912171; 1698775; 17000679; 17088321; 17096442; 17178858; 17178873; 17182940; 17269766; 17357518; 17373931; 17473191; 17574772; 17607721; 17706587; 17727250; 17997411; 18001475; 18001704; 18006768; 18052707; 18091353; 18155181; 18259971; 18308831; 18324629; 18334288; 18390828; 18396640; 18403602; 18425585; 18465858; 18539597; 18617639; 18619044; 18660381; 1874716; 18823978; 18988744; 19056482; 19132754; 19159011; 19239231; 19258954; 19275207; 19293200; 19321798; 19420105; 19562509; 19578796; 19590686; 19628284; 19643940; 19664242; 19703773; 19731200; 19789190; 19794969; 19812315; 19913121; 19932771; 19958990; 20018959; 20041641; 20078883; 20160424; 20230842; 20345904; 20376807; 20392358; 20415416; 20452482; 20484597; 20485444; 20546881; 20587546; 20595276; 20628086; 20655856; 20673868; 20736794; 20817735; 20827277; 20965620; 21048031; 21055468; 21277817; 21410539; 21593211; 21606841; 21683576; 2169335; 21730350; 21920892; 21967233; 22076168; 22117411; 22119538; 22153340; 22305682; 22528292; 2253219; 22689580; 22863605; 22907031; 22936257; 23075521; 23271741; 23343195; 23343931; 23357697; 23567804; 23575435; 23583775; 23642232; 23898086; 23900981; 24043512; 24146820; 24398311; 24424266; 24432723; 24784232; 24834994; 24885469; 24914938; 25006744; 25078452; 25412686; 2548603; 2551898; 26040769; 26120586; 26608672; 26887942; 27329669; 27345464; 27356908; 27377745; 27391467; 27564088; 27746079; 27807143; 27987113; 27996256; 28098914; 28122331; 28343758; 2834383; 28385529; 2845110; 28551623; 28655442; 28692348; 28958661; 28990117; 29048889; 29101312; 29317790; 29390099; 29429629; 29458338; 29727184; 29906531; 29925830; 30658596; 30691826; 30789935; 3095317; 31304819; 31499120; 31711716; 31862687; 3223920; 32650441; 32702535; 33065600; 33404658; 33892690; 33902302; 34384863; 34459757; 6258630; 7547873; 8216228; 8223643; 8380588; 8463259; 8603731; 8626565; 8920930; 9065415; 9092507; 9428515; 9651395; |
| Motif | MOTIF 90..97; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 54,002 |
| Kinetics | |
| Metal Binding | METAL 92; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 124; /note=Calcium 1; METAL 158; /note=Calcium 2; METAL 168; /note=Zinc 1; METAL 170; /note=Zinc 1; METAL 175; /note=Calcium 3; METAL 176; /note=Calcium 3; via carbonyl oxygen; METAL 178; /note=Calcium 3; via carbonyl oxygen; METAL 180; /note=Calcium 3; via carbonyl oxygen; METAL 183; /note=Zinc 1; METAL 190; /note=Calcium 2; via carbonyl oxygen; METAL 192; /note=Calcium 2; via carbonyl oxygen; METAL 194; /note=Calcium 2; METAL 196; /note=Zinc 1; METAL 198; /note=Calcium 3; METAL 199; /note=Calcium 1; METAL 201; /note=Calcium 1; METAL 201; /note=Calcium 3; METAL 218; /note=Zinc 2; catalytic; METAL 222; /note=Zinc 2; catalytic; METAL 228; /note=Zinc 2; catalytic; METAL 289; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 333; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 381; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 430; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.65; |