ArticleThe Journal of biological chemistry2008
Crystal structure of human plasma platelet-activating factor acetylhydrolase: structural implication to lipoprotein binding and catalysis.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 82 citations in OpenAlex.
- Lipoprotein-associated phospholipase A2 (Lp-PLA2): a key hub linking lipid metabolism and immune inflammation.Frontiers in immunology · 2026Review
- Gallic Acid as a Non-Selective Inhibitor of α/β-Hydrolase Fold Enzymes Involved in the Inflammatory Process: The Two Sides of the Same Coin.Pharmaceutics · 2022Article
- Lipoprotein-associated phospholipase AProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Lipoprotein-associated phospholipase A2: The story continues.Medicinal research reviews · 2020Review
- Structural Modeling of Wild and Mutant Forms of Human Plasma Platelet Activating Factor-Acetyl Hydrolase Enzyme.Journal of inflammation research · 2020Article
- Human Secretary Phospholipase A2 Mutations and Their Clinical Implications.Journal of inflammation research · 2020Review
- Phospholipase A2 is an Inflammatory Predictor in Cardiovascular Diseases: Is there any Spacious Room to Prove the Causation?Current cardiology reviews · 2020Review
- Loop of Streptomyces Feruloyl Esterase Plays an Important Role in the Enzyme's Catalyzing the Release of Ferulic Acid from Biomass.Applied and environmental microbiology · 2018Article
- Exploration of Adhesion Molecule Expression in Cardiac Muscle of Early Atherosclerosis Dyslipidemic Sprague Dawley Rats.The open medicinal chemistry journal · 2018Article
- Review of four major distinct types of human phospholipase AAdvances in biological regulation · 2018Review
- Investigation of a Bicyclo[1.1.1]pentane as a Phenyl Replacement within an LpPLAACS medicinal chemistry letters · 2017Article
- A robust all-atom model for LCAT generated by homology modeling.Journal of lipid research · 2015Article
- Selective inhibitors and tailored activity probes for lipoprotein-associated phospholipase A(2).Bioorganic & medicinal chemistry letters · 2013Article
- Using hydrogen/deuterium exchange mass spectrometry to define the specific interactions of the phospholipase A2 superfamily with lipid substrates, inhibitors, and membranes.The Journal of biological chemistry · 2013Review
- Sequencing of Lp-PLA2-encoding PLA2G7 gene in 2000 Europeans reveals several rare loss-of-function mutations.The pharmacogenomics journal · 2012Article
- Modulation of oxidative stress, inflammation, and atherosclerosis by lipoprotein-associated phospholipase A2.Journal of lipid research · 2012Review
- FunSAV: predicting the functional effect of single amino acid variants using a two-stage random forest model.PloS one · 2012Article
- Phospholipase A2 enzymes: physical structure, biological function, disease implication, chemical inhibition, and therapeutic intervention.Chemical reviews · 2011Review
- Intracellular erythrocyte platelet-activating factor acetylhydrolase I inactivates aspirin in blood.The Journal of biological chemistry · 2011Article
- Trafficking of platelet-activating factor acetylhydrolase type II in response to oxidative stress.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Human plasma platelet-activating factor (PAF) acetylhydrolase functions by reducing PAF levels as a general anti-inflammatory scavenger and is linked to anaphylactic shock, asthma, and allergic reactions. The enzyme has also been implicated in hydrolytic activities of other pro-inflammatory agents, such as sn-2 oxidatively fragmented phospholipids. This plasma enzyme is tightly bound to low and high density lipoprotein particles and is also referred to as lipoprotein-associated phospholipase A2. The crystal structure of this enzyme has been solved from x-ray diffraction data collected to a resolution of 1.5 angstroms. It has a classic lipase alpha/beta-hydrolase fold, and it contains a catalytic triad of Ser273, His351, and Asp296. Two clusters of hydrophobic residues define the probable interface-binding region, and a prediction is given of how the enzyme is bound to lipoproteins. Additionally, an acidic patch of 10 carboxylate residues and a neighboring basic patch of three residues are suggested to play a role in high density lipoprotein/low density lipoprotein partitioning. A crystal structure is also presented of PAF acetylhydrolase reacted with the organophosphate compound paraoxon via its active site Ser273. The resulting diethyl phosphoryl complex was used to model the tetrahedral intermediate of the substrate PAF to the active site. The model of interface binding begins to explain the known specificity of lipoprotein-bound substrates and how the active site can be both close to the hydrophobic-hydrophilic interface and at the same time be accessible to the aqueous phase.
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