| IED ID | IndEnz0002004249 |
| Enzyme Type ID | protease004249 |
| Protein Name |
Hementin EC 3.4.24.- Fragments |
| Gene Name | |
| Organism | Haementeria ghilianii (Amazon leech) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Spiralia Lophotrochozoa Annelida Clitellata Hirudinea (leeches) Rhynchobdellida Glossiphoniidae Haementeria Haementeria ghilianii (Amazon leech) |
| Enzyme Sequence | TTLTEPEPDLTYLTFVXIVXXEMPIFVMATANSGITSTF |
| Enzyme Length | 39 |
| Uniprot Accession Number | Q7M3P9 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA, cysteine, DTT and sodium phosphate. Partially inhibited by EGTA, citrate, Tris and glycine. Not inhibited by DFP, PMSF, iodacetic acid and leupeptin. Requires sodium chloride concentrations higher than 0.15 M for activity. {ECO:0000269|PubMed:1772983, ECO:0000269|PubMed:6361187}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Metalloprotease with anticoagulant activity. Cleaves fibrinogen Aalpha (FGA), gamma (FGG) and Bbeta (FGB) chains after positions 'Asn-121', 'Lys-160' and 'Pro-102', respectively. Breaks down cross-linked and non-cross-linked fibrin clots. Prevents and reverts platelet aggregation induced by ADP and collagen. Prevents thrombin-induced platelet clotting. Does not affect plasma levels of coagulation factors prothrombin (F2), V (F5), VII (F7), VIII (F8), IX (F9), X (F10), XI (F11), XII (F12), plasma kallikrein (KLKB1) and kininogen-1 (KNG1). {ECO:0000269|PubMed:1450340, ECO:0000269|PubMed:1772983, ECO:0000269|PubMed:2143188, ECO:0000269|PubMed:2187898, ECO:0000269|PubMed:6361187, ECO:0000269|PubMed:6387015, ECO:0000269|PubMed:9184410, ECO:0000269|PubMed:9282793, ECO:0000269|Ref.7}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Active at 37 degrees Celsius. Activity reversibly reduced to 26% and 0% at 25 degrees Celsius and 4 degrees Celsius, respectively. Complete and irreversible loss of activity after 15 min at 60 degrees Celsius. {ECO:0000269|PubMed:6361187, ECO:0000269|PubMed:6387015}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. Active from pH 5.5 to 11. {ECO:0000269|PubMed:6361187, ECO:0000269|PubMed:6387015}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Non-adjacent residues (1); Non-terminal residue (1) |
| Keywords | Blood coagulation;Direct protein sequencing;Fibrinolysis;Hemostasis;Hydrolase;Metalloprotease;Protease;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.7}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 4,286 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 uM for fibrinogen {ECO:0000269|PubMed:6361187, ECO:0000269|PubMed:6387015}; Vmax=26 nmol/min/mg enzyme with fibrinogen as substrate {ECO:0000269|PubMed:6361187, ECO:0000269|PubMed:6387015}; Vmax=2.4 pmol/sec/mg enzyme with cross-linked fibrin clots as substrate (with enzyme incorporated in clot) {ECO:0000269|PubMed:6361187, ECO:0000269|PubMed:6387015}; Vmax=2.6 pmol/sec/mg enzyme with non-cross-linked fibrin clots as substrate (with enzyme incorporated in clot) {ECO:0000269|PubMed:6361187, ECO:0000269|PubMed:6387015}; Vmax=0.011 pmol/sec/mg enzyme with cross-linked fibrin clots as substrate (with enzyme external to clot) {ECO:0000269|PubMed:6361187, ECO:0000269|PubMed:6387015}; Vmax=0.05 pmol/sec/mg enzyme with non-cross-linked fibrin clots as substrate (with enzyme external to clot) {ECO:0000269|PubMed:6361187, ECO:0000269|PubMed:6387015}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |