IED ID | IndEnz0002014246 |
Enzyme Type ID | protease014246 |
Protein Name |
Clotting factor B EC 3.4.21.85 Coagulation factor B Cleaved into: Clotting factor B light chain; Clotting factor B heavy chain |
Gene Name | |
Organism | Tachypleus tridentatus (Japanese horseshoe crab) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Chelicerata Merostomata (horseshoe crabs) Xiphosura Limulidae Tachypleus Tachypleus tridentatus (Japanese horseshoe crab) |
Enzyme Sequence | MTWICVITLFALASATLGNKVSRVGVLFPKTRNDNECTARGGLKGSCKSLIDCPSVLATLKDSFPVVCSWNGRFQPIVCCPDAIAPPPVTTTAVTVISTKEPKLPRLHISGCGKRKVKIDITTVGRSGSPILPPISTPQNSTGGRGIIAGGVEAKIGAWPWMAAVFVKNFGIGRFHCAGSIISNKYILSAAHAFLIGGRKLTPTRLAVRVGGHYIKRGQEYPVKDVIIHPHYVEKENYNDIAIIELKEELNFTDLVNPICLPDPETVTDPLKDRIVTAAGWGDLDFSGPRSQVLREVSIPVVPVDKCDQAYEKLNTPSLKNGITNNFLCAGLEEGGKDACQGDSGGPLMLVNNTRWIVVGVVSFGHKCAEEGYPGVYSRVASYLDWIAKVTNSLDHAVTN |
Enzyme Length | 400 |
Uniprot Accession Number | Q27081 |
Absorption | |
Active Site | ACT_SITE 192; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P26262; ACT_SITE 240; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P26262; ACT_SITE 344; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P26262 |
Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by alpha2-plasmin inhibitor and DFP. Partially inhibited by benzamidine, leupeptin and PCMB. {ECO:0000269|PubMed:3519594}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Selective cleavage of 98-Arg-|-Ile-99 bond in Limulus proclotting enzyme to form active clotting enzyme.; EC=3.4.21.85; Evidence={ECO:0000269|PubMed:2266134}; |
DNA Binding | |
EC Number | 3.4.21.85 |
Enzyme Function | FUNCTION: This enzyme is closely associated with an endotoxin-sensitive hemolymph coagulation system which may play important roles in both hemostasis and host defense mechanisms. Its active form catalyzes the activation of proclotting enzyme. Does not activate the mammalian coagulation factors factor IX, factor X, prothrombin, plasminogen, protein C or prekallikrein. Does not hydrolyze fibrinogen. Does not catalyze the activation of factor C or coagulogen. {ECO:0000269|PubMed:2266134, ECO:0000269|PubMed:3519594}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (2); Disulfide bond (5); Domain (2); Glycosylation (3); Propeptide (1); Signal peptide (1) |
Keywords | Direct protein sequencing;Disulfide bond;Glycoprotein;Hemolymph clotting;Hydrolase;Protease;Secreted;Serine protease;Signal;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Note=Secreted in hemolymph. {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000269|PubMed:8407978 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 43,049 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=0.9 umol/min/mg enzyme toward Boc-Val-Pro-Arg-MCA {ECO:0000269|PubMed:3519594}; Vmax=0.1 umol/min/mg enzyme toward Boc-Ile-Glu-Gly-Arg-MCA {ECO:0000269|PubMed:3519594}; Vmax=0.2 umol/min/mg enzyme toward Boc-Leu-Ser-Thr-Arg-MCA {ECO:0000269|PubMed:3519594}; Vmax=0.1 umol/min/mg enzyme toward Boc-Leu-Gly-Arg-MCA {ECO:0000269|PubMed:3519594}; Vmax=1.1 umol/min/mg enzyme toward Bz-Thr-Ser-Arg-MCA {ECO:0000269|PubMed:3519594}; Vmax=0.7 umol/min/mg enzyme toward Bz-Ser-Ser-Arg-MCA {ECO:0000269|PubMed:3519594}; Vmax=1.3 umol/min/mg enzyme toward Bz-Ser-Thr-Arg-MCA {ECO:0000269|PubMed:3519594}; Vmax=1.9 umol/min/mg enzyme toward Bz-Thr-Thr-Arg-MCA {ECO:0000269|PubMed:3519594}; Vmax=1.1 umol/min/mg enzyme toward Boc-Leu-Thr-Arg-MCA {ECO:0000269|PubMed:3519594}; Vmax=2.1 umol/min/mg enzyme toward Boc-Met-Thr-Arg-MCA {ECO:0000269|PubMed:3519594}; Vmax=1.2 umol/min/mg enzyme toward Boc-Gln-Arg-Arg-MCA {ECO:0000269|PubMed:3519594}; Vmax=0.6 umol/min/mg enzyme toward Boc-Asp-Pro-Arg-MCA {ECO:0000269|PubMed:3519594}; |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |