| IED ID | IndEnz0005000765 |
| Enzyme Type ID | lipase000765 |
| Protein Name |
Platelet-activating factor acetylhydrolase 2, cytoplasmic EC 3.1.1.47 PAF:lysophospholipid transacetylase PAF:sphingosine transacetylase Platelet-activating factor acetyltransferase PAFAH2 EC 2.3.1.149 Serine-dependent phospholipase A2 SD-PLA2 hSD-PLA2 |
| Gene Name | PAFAH2 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MGVNQSVGFPPVTGPHLVGCGDVMEGQNLQGSFFRLFYPCQKAEETMEQPLWIPRYEYCTGLAEYLQFNKRCGGLLFNLAVGSCRLPVSWNGPFKTKDSGYPLIIFSHGLGAFRTLYSAFCMELASRGFVVAVPEHRDRSAATTYFCKQAPEENQPTNESLQEEWIPFRRVEEGEKEFHVRNPQVHQRVSECLRVLKILQEVTAGQTVFNILPGGLDLMTLKGNIDMSRVAVMGHSFGGATAILALAKETQFRCAVALDAWMFPLERDFYPKARGPVFFINTEKFQTMESVNLMKKICAQHEQSRIITVLGSVHRSQTDFAFVTGNLIGKFFSTETRGSLDPYEGQEVMVRAMLAFLQKHLDLKEDYNQWNNLIEGIGPSLTPGAPHHLSSL |
| Enzyme Length | 392 |
| Uniprot Accession Number | Q99487 |
| Absorption | |
| Active Site | ACT_SITE 236; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P79106; ACT_SITE 259; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 314; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by phenylmethanesulfonyl fluoride, 3,4,dichloroisocoumarin, diisopropyl fluorophosphate (DFP) and diethyl p-nitrophenyl phosphate (DENP). {ECO:0000269|PubMed:9494101}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47; Evidence={ECO:0000269|PubMed:9494101};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778; Evidence={ECO:0000269|PubMed:9494101}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496; Evidence={ECO:0000250|UniProtKB:P83006};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480; Evidence={ECO:0000250|UniProtKB:P83006}; CATALYTIC ACTIVITY: Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + 1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine = 1-O-(1Z-alkenyl)-2-acetyl-sn-glycero-3-phosphoethanolamine + 1-O-hexadecyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41396, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496, ChEBI:CHEBI:77288, ChEBI:CHEBI:78419; Evidence={ECO:0000250|UniProtKB:P83006};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41397; Evidence={ECO:0000250|UniProtKB:P83006}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + sphing-4-enine = 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+) + N-(acetyl)-sphing-4-enine; Xref=Rhea:RHEA:41408, ChEBI:CHEBI:15378, ChEBI:CHEBI:44811, ChEBI:CHEBI:46979, ChEBI:CHEBI:57756, ChEBI:CHEBI:64496; Evidence={ECO:0000250|UniProtKB:P83006};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41409; Evidence={ECO:0000250|UniProtKB:P83006}; CATALYTIC ACTIVITY: Reaction=1-organyl-2-lyso-sn-glycero-3-phospholipid + a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine = 1-O-alkyl-sn-glycero-3-phosphocholine + 1-organyl-2-acetyl-sn-glycero-3-phospholipid; Xref=Rhea:RHEA:11048, ChEBI:CHEBI:685, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707, ChEBI:CHEBI:76590; EC=2.3.1.149; Evidence={ECO:0000250|UniProtKB:P83006};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11049; Evidence={ECO:0000250|UniProtKB:P83006}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-glutaryl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + glutarate + H(+); Xref=Rhea:RHEA:41700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30921, ChEBI:CHEBI:64496, ChEBI:CHEBI:78371; Evidence={ECO:0000250|UniProtKB:P79106};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41701; Evidence={ECO:0000250|UniProtKB:P79106}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-succinyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+) + succinate; Xref=Rhea:RHEA:41696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:64496, ChEBI:CHEBI:78369; Evidence={ECO:0000250|UniProtKB:P79106};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41697; Evidence={ECO:0000250|UniProtKB:P79106}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-butanoyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + butanoate + H(+); Xref=Rhea:RHEA:41692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:64496, ChEBI:CHEBI:78368; Evidence={ECO:0000250|UniProtKB:P79106};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41693; Evidence={ECO:0000250|UniProtKB:P79106}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-propanoyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+) + propanoate; Xref=Rhea:RHEA:41688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17272, ChEBI:CHEBI:64496, ChEBI:CHEBI:78367; Evidence={ECO:0000250|UniProtKB:P79106};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41689; Evidence={ECO:0000250|UniProtKB:P79106}; |
| DNA Binding | |
| EC Number | 3.1.1.47; 2.3.1.149 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolyze of the acetyl group at the sn-2 position of platelet-activating factor (PAF) and its analogs, leading to their inactivation (PubMed:9494101). Hydrolyzes propionyl and butyroyl moieties approximately half as effectively as PAF (By similarity). Also catalyzes transacetylation of the acetyl group from platelet-activating factor (PAF) to lysoplasmalogen and to sphingosine, producing plasmalogen analogs of PAF and N-acetylsphingosine (C2-ceramide) respectively. Has a marked selectivity for phospholipids with short acyl chains at the sn-2 position (By similarity). {ECO:0000250|UniProtKB:P79106, ECO:0000250|UniProtKB:P83006, ECO:0000269|PubMed:9494101}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Initiator methionine (1); Lipidation (1); Sequence conflict (1) |
| Keywords | Cytoplasm;Endoplasmic reticulum;Hydrolase;Lipid degradation;Lipid metabolism;Lipoprotein;Membrane;Myristate;Reference proteome;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9494101}. Membrane {ECO:0000250|UniProtKB:P79106}; Lipid-anchor {ECO:0000250|UniProtKB:P79106}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P79106}; Lipid-anchor {ECO:0000250|UniProtKB:P79106}. Note=In resting cells, localizes to intracellular membranes and cytoplasm. Translocates from the cytoplasm to intracellular membranes upon oxidative stress. {ECO:0000250|UniProtKB:P79106}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11294621; 12406338; 16650870; 17157859; 17272759; 21882811; 25707358; 26791393; |
| Motif | |
| Gene Encoded By | |
| Mass | 44,036 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=42 uM for 2-O-acetyl-1-O-hexadecyl-sn-glycero-3-phosphocholine (PAF) {ECO:0000269|PubMed:9494101}; KM=10 uM for 1-decanoyl-2-(4-nitrophenylglutaryl) phosphate (DNGP) {ECO:0000269|PubMed:9494101}; Vmax=35 umol/min/mg enzyme with 2-O-acetyl-1-O-hexadecyl-sn-glycero-3-phosphocholine (PAF) as substrate {ECO:0000269|PubMed:9494101}; Vmax=1.7 umol/min/mg enzyme with 1-decanoyl-2-(4-nitrophenylglutaryl) phosphate (DNGP) as substrate {ECO:0000269|PubMed:9494101}; |
| Metal Binding | |
| Rhea ID | RHEA:17777; RHEA:17778; RHEA:40479; RHEA:40480; RHEA:41396; RHEA:41397; RHEA:41408; RHEA:41409; RHEA:11048; RHEA:11049; RHEA:41700; RHEA:41701; RHEA:41696; RHEA:41697; RHEA:41692; RHEA:41693; RHEA:41688; RHEA:41689 |
| Cross Reference Brenda | 3.1.1.47; |