Detail Information for IndEnz0002012580
IED ID IndEnz0002012580
Enzyme Type ID protease012580
Protein Name Snake venom serine protease AHP-Ka
SVSP
EC 3.4.21.-
Fragment
Gene Name
Organism Gloydius halys (Chinese water mocassin) (Agkistrodon halys)
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) Gloydius Gloydius halys (Chinese water mocassin) (Agkistrodon halys)
Enzyme Sequence VIGGDECNINEHRFL
Enzyme Length 15
Uniprot Accession Number P0DJG5
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Inhibited by PMSF, Fe(3+), Fe(2+), Cu(2+), Cd(2+), Mn(2+), and Al(3+). Not inhibited by Ca(2+) and Mg(2+) and EDTA. {ECO:0000269|PubMed:22162083}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.21.-
Enzyme Function FUNCTION: Snake venom serine protease that hydrolyzes specific chromogenic substrate S-2302 suggesting that AHP-Ka is a plasma kallikrein. Has esterase activity on alpha-N-benzoyl-L-arginine ethyl ester hydrochloride (BAEE) and amidolytic activity. {ECO:0000269|PubMed:22162083}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-40 degrees Celsius. {ECO:0000269|PubMed:22162083};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8. {ECO:0000269|PubMed:22162083};
Pathway
nucleotide Binding
Features Chain (1); Disulfide bond (1); Domain (1); Non-terminal residue (1)
Keywords Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Secreted;Serine protease;Toxin
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification PTM: N-glycosylated. Cleavage of N-glycans reduces the catalytic enzymatic efficiency.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 1,716
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda