Detail Information for IndEnz0002010298
IED ID IndEnz0002010298
Enzyme Type ID protease010298
Protein Name Zinc metalloproteinase alsophinase
EC 3.4.24.-
Snake venom metalloproteinase
SVMP
Fragment
Gene Name
Organism Borikenophis portoricensis (Puerto Rican racer) (Alsophis portoricensis)
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 Dipsadidae Borikenophis Borikenophis portoricensis (Puerto Rican racer) (Alsophis portoricensis)
Enzyme Sequence QDTYLNAKKYIEFYLVVDNGMFXKYSXXFTV
Enzyme Length 31
Uniprot Accession Number P0DJH4
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Inhibited by 1,10-phenanthroline. {ECO:0000269|PubMed:22349739}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: Snake venom zinc metalloprotease that has potent hemorrhagic activity, fibrinogenolytic activity on the alpha-subunit of human fibrinogen (FGA) in vitro and provokes necrosis in skin, muscle and lung tissues. May contribute to local edema and ecchymosis induced by venom. Hydrolyzes model substrate (beta-chain of insulin) at Ala(14)-Leu(15). {ECO:0000269|PubMed:22349739}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Domain (1); Metal binding (1); Modified residue (1); Non-terminal residue (1)
Keywords Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Myotoxin;Protease;Pyrrolidone carboxylic acid;Secreted;Toxin;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue MOD_RES 1; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:22349739
Post Translational Modification PTM: Contains 9 disulfide bonds. {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 3,732
Kinetics
Metal Binding METAL 12; /note=Calcium; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda