Detail Information for IndEnz0002001167
IED ID IndEnz0002001167
Enzyme Type ID protease001167
Protein Name Basic phospholipase A2 T1-2 A chain
svPLA2
EC 3.1.1.4
Phosphatidylcholine 2-acylhydrolase T1-2 A
Fragment
Gene Name
Organism Bungarus candidus (Malayan krait)
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 Elapidae Bungarinae Bungarus Bungarus candidus (Malayan krait)
Enzyme Sequence NLYQFKEMIRYTIP
Enzyme Length 14
Uniprot Accession Number P84472
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:P00617, ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
DNA Binding
EC Number 3.1.1.4
Enzyme Function FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini and exhibits indirect hemolytic activity against human erythrocytes. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:14769867}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Non-terminal residue (1)
Keywords Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Neurotoxin;Presynaptic neurotoxin;Secreted;Toxin
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14769867}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 1,816
Kinetics
Metal Binding
Rhea ID RHEA:15801
Cross Reference Brenda