Detail Information for IndEnz0005000975
IED ID IndEnz0005000975
Enzyme Type ID lipase000975
Protein Name Lipase member H-B
EC 3.1.1.-
Gene Name liph-b
Organism Xenopus laevis (African clawed frog)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog)
Enzyme Sequence MLLSFYFNGLLLVGCLLSWGRSDTEGQCHSFTDLNIHNSIIGTALKVQLLLYTPENPKCAQDLNEDNSTGFQYLNVTRKTVFITHGYRPTGSPPVWIDNIVTKFLDIQDFNVILVDWNRGATTVLYHNAAAKTRKVADILKRLIDNMLSQGATLDSIYMVGVSLGAHISGFVGKMYNGSIGRITGLDPAGPLFNGKPPEERLHYTDAQFVDVVHTDTDGLGYKESLGHIDFYPNGGTDQPGCPKTILSGSEYFKCDHQRSVFLYIASLTNNGDLVGFPCKSYRDYRIGNCTNCKEFLPLSCPVFGFYADKWKDHLVKKNPPGTKAFFDTAAKDPFCIFHYYLDIMTWSSQTRRGYITIRLMSLNGNVTESKLDKDHATFEQYKEVSLLAKFDQDLDPMTRISVTFTTGSVIGPKFKLRVLRMRLRPLTNTNRPILCRYDFVLLENVEMEFNPIPCEDTNL
Enzyme Length 460
Uniprot Accession Number Q641F6
Absorption
Active Site ACT_SITE 163; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 187; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 257; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + hexadecanoate; Xref=Rhea:RHEA:40943, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64839, ChEBI:CHEBI:77593; Evidence={ECO:0000250|UniProtKB:Q8WWY8};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40944; Evidence={ECO:0000250|UniProtKB:Q8WWY8};
DNA Binding
EC Number 3.1.1.-
Enzyme Function FUNCTION: Hydrolyzes specifically phosphatidic acid (PA) to produce 2-acyl lysophosphatidic acid (LPA; a potent bioactive lipid mediator) and fatty acid (By similarity). Does not hydrolyze other phospholipids, like phosphatidylserine (PS), phosphatidylcholine (PC) and phosphatidylethanolamine (PE) or triacylglycerol (TG) (By similarity). {ECO:0000250|UniProtKB:Q8WWY8}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (4); Glycosylation (5); Signal peptide (1)
Keywords Cell membrane;Disulfide bond;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Membrane;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8WWY8}. Cell membrane {ECO:0000250|UniProtKB:Q8WWY8}; Peripheral membrane protein.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..26; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 51,890
Kinetics
Metal Binding
Rhea ID RHEA:40943; RHEA:40944
Cross Reference Brenda