| IED ID | IndEnz0002011951 |
| Enzyme Type ID | protease011951 |
| Protein Name |
Snake venom metalloproteinase HF-1 BmHF-1 SVMP EC 3.4.24.- |
| Gene Name | |
| Organism | Bothrops marajoensis (Marajo lancehead) |
| 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) Bothrops Bothrops marajoensis (Marajo lancehead) |
| Enzyme Sequence | PCWKGWSEDEQNLWPQRYIQLVVVADHGMFMKYNGDLAAIRKRVHELVNNINGFYRSLNIDVSLTDLEIWSDQDFITVVQSSSAKNTLNSFGEWREADLLRRKSHDHAQLLTAIDLDDDTVGLAYTSSMCNPRKSVAWGQDHSEEPINLLDVGVTMAHELGHNLGMNHDEEKKCHCGASLCIMSPSITEGPSLEFSDDSMGYYQSFLVVVNYNPQCILNKPEDQYYYILSPKHRIYSW |
| Enzyme Length | 238 |
| Uniprot Accession Number | P86802 |
| Absorption | |
| Active Site | ACT_SITE 159; /evidence="ECO:0000250|UniProtKB:P15167, ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA and EGTA. Inhibited by serum and antihemorrhagic factors Da2-I and Da2-II from D.albiventris. Not inhibited by PMSF or SBT-I. {ECO:0000269|PubMed:20607373}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloprotease that is weakly hemorrhagic and has Aalpha, Bbeta fibrinogenolytic activities. Cleaves the Aalpha chain of fibrinogen first, followed by the Bbeta chain and shows no effect on the gamma chain. Has caseinolytic activity. Induces dose-dependent edema. {ECO:0000269|PubMed:20607373}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature for caseinolytic activity is 40 degrees Celsius. Activity decreases rapidly at higher or lower temperatures. No activity below 10 degrees Celsius or above 70 degrees Celsius. {ECO:0000269|PubMed:20607373}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. Activity decreases rapidly at higher or lower pH. {ECO:0000269|PubMed:20607373}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Domain (1); Metal binding (6) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20607373}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 27,266 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=7.51 umol/min/mg enzyme with casein as substrate {ECO:0000269|PubMed:20607373}; |
| Metal Binding | METAL 106; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P15167; METAL 158; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P15167; METAL 162; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P15167; METAL 168; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P15167; METAL 216; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P15167; METAL 219; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P15167 |
| Rhea ID | |
| Cross Reference Brenda |