| IED ID | IndEnz0002011824 |
| Enzyme Type ID | protease011824 |
| Protein Name |
Snake venom metalloproteinase TM-1 SVMP EC 3.4.24.- Zinc-dependent metalloproteinase |
| Gene Name | |
| Organism | Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Episquamata Toxicofera Serpentes (snakes) Colubroidea Viperidae Crotalinae (pit vipers) Protobothrops Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus) |
| Enzyme Sequence | QQRFPQRYVMLAIVADHGMVTKYSGNSSAITTRVHQMVSHVTEMYSPLNIATTLSLLRIWSSKDLITVQSDSSVTLGSFGDWRKVVLLSQQAHDCAFLNTATALDDSTIGLAYSNGMCDPKFSVGLVQDHSSNVFMVAVTMTHELGHNLGMAHDEAGGCACSSCIMSPAASSGPSKLFSDCSKDDYQTFLTNTNPQCILNAP |
| Enzyme Length | 202 |
| Uniprot Accession Number | U3KRG1 |
| Absorption | |
| Active Site | ACT_SITE 144; /evidence=ECO:0000305|PubMed:23732127 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA and 1,10-phenanthroline (PubMed:8193588). Is also inhibited by endogenous tripeptide inhibitors pyroGlu-Asn-Trp, pyroGlu-Gln-Trp, and pyroGlu-Lys-Trp (PubMed:9703966). {ECO:0000269|PubMed:8193588, ECO:0000269|PubMed:9703966}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Potent fibrinogenolytic protease which cleaves mainly the Aalpha (FGA) and Bbeta (FGB) chains of fibrinogen and slightly the gamma chain (FGG) (PubMed:8193588, PubMed:7488093). Shows preference for substrates having a moderate-size and hydrophobic residue at the P1' position. Preferentially cleaves Ala-|-Leu and Tyr-|-Leu bonds (PubMed:23732127). Is more susceptible to tripeptide inhibitors than TM-3 (AC O57413) (PubMed:9703966). {ECO:0000269|PubMed:23732127, ECO:0000269|PubMed:7488093, ECO:0000269|PubMed:8193588, ECO:0000269|PubMed:9703966}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (6); Chain (1); Disulfide bond (3); Domain (1); Helix (8); Metal binding (3); Modified residue (1); Sequence conflict (1); Turn (3) |
| Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Protease;Pyrrolidone carboxylic acid;Secreted;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7488093, ECO:0000269|PubMed:8193588}. |
| Modified Residue | MOD_RES 1; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000305|PubMed:7488093, ECO:0000305|PubMed:8193588" |
| Post Translational Modification | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:7488093}.; PTM: Not glycosylated. {ECO:0000269|PubMed:23732127}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4J4M; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 21,791 |
| Kinetics | |
| Metal Binding | METAL 143; /note=Zinc; catalytic; via tele nitrogen; /evidence=ECO:0007744|PDB:4J4M; METAL 147; /note=Zinc; catalytic; via tele nitrogen; /evidence=ECO:0007744|PDB:4J4M; METAL 153; /note=Zinc; via tele nitrogen; /evidence=ECO:0007744|PDB:4J4M |
| Rhea ID | |
| Cross Reference Brenda |