Detail Information for IndEnz0002014246
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