ArticleThe Journal of biological chemistry2011
Purification, identification, and cloning of lysoplasmalogenase, the enzyme that catalyzes hydrolysis of the vinyl ether bond of lysoplasmalogen.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 62 citations in OpenAlex.
- The Changes in Plasmalogens: Chemical Diversity and Nutritional Implications-A Narrative Review.Nutrients · 2025Review
- SPNS1 variants cause multiorgan disease and implicate lysophospholipid transport as critical for mTOR-regulated lipid homeostasis.The Journal of clinical investigation · 2025Article
- Alterations in ether lipid metabolism in obesity revealed by systems genomics of multi-omics datasets.PLoS biology · 2025Article
- Modulation of endogenous plasmalogens by genetic ablation of lysoplasmalogenase (Tmem86b) in mice.Journal of lipid research · 2025Article
- Early Gestational Hepatic Lipidomic Profiles Are Modulated by One-Carbon Metabolite Supplementation and Nutrient Restriction in Beef Heifers and Fetuses.Metabolites · 2025Article
- Sex differences in the lipid profiles of visceral adipose tissue with obesity and gonadectomy.Journal of lipid research · 2025Article
- Constructing a novel mitochondrial metabolism-related genes signature to evaluate tumor immune microenvironment and predict survival of colorectal cancer.Frontiers in medicine · 2025Article
- Zebrafish are resilient to the loss of major diacylglycerol acyltransferase enzymes.The Journal of biological chemistry · 2024Article
- Characterizing lipid constituents of B. moojeni snake venom: a comparative approach for chemical and biological investigations.Archives of toxicology · 2024Article
- Genome-wide loss-of-function screen using human pluripotent stem cells to study virus-host interactions for SARS-CoV-2.Stem cell reports · 2023Article
- Marine Plasmalogens: A Gift from the Sea with Benefits for Age-Associated Diseases.Molecules (Basel, Switzerland) · 2023Review
- Article
- Acid-Functionalized Artificial Enzymes with Tunable Selectivity for Vinyl Ether Hydrolysis.The Journal of organic chemistry · 2023Article
- Peroxisomes Are Highly Abundant and Heterogeneous in Human Parotid Glands.International journal of molecular sciences · 2023Article
- Latest advances in the regulatory genes of adipocyte thermogenesis.Frontiers in endocrinology · 2023Review
- Transcriptional Profiles Analysis of COVID-19 and Malaria Patients Reveals Potential Biomarkers in Children.bioRxiv : the preprint server for biology · 2022Article
- Adipocyte lysoplasmalogenase TMEM86A regulates plasmalogen homeostasis and protein kinase A-dependent energy metabolism.Nature communications · 2022Article
- Mycobacterium tuberculosis encodes a YhhN family membrane protein with lysoplasmalogenase activity that protects against toxic host lysolipids.The Journal of biological chemistry · 2022Article
- Plasmalogens and Photooxidative Stress Signaling in Myxobacteria, and How it Unmasked CarF/TMEM189 as the Δ1'-Desaturase PEDS1 for Human Plasmalogen Biosynthesis.Frontiers in cell and developmental biology · 2022Review
- Plasmalogens Eliminate Aging-Associated Synaptic Defects and Microglia-Mediated Neuroinflammation in Mice.Frontiers in molecular biosciences · 2022Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Lysoplasmalogenase (EC 3.3.2.2 and EC 3.3.2.5) is an enzyme that catalyzes hydrolytic cleavage of the vinyl ether bond of lysoplasmalogen, forming fatty aldehyde and glycerophosphoethanolamine or glycerophosphocholine and is specific for the sn-2-deacylated form of plasmalogen. Here we report the purification, characterization, identification, and cloning of lysoplasmalogenase. Rat liver microsomal lysoplasmalogenase was solubilized with octyl glucoside and purified 500-fold to near homogeneity using four chromatography steps. The purified enzyme has apparent K(m) values of ∼50 μm for both lysoplasmenylcholine and lysoplasmenylethanolamine and apparent V(m) values of 24.5 and 17.5 μmol/min/mg protein for the two substrates, respectively. The pH optimum was 7.0. Lysoplasmalogenase was competitively inhibited by lysophosphatidic acid (K(i) ∼20 μm). The predominant band on a gel at ∼19 kDa was subjected to trypsinolysis, and the peptides were identified by mass spectrometry as Tmem86b, a protein of unknown function. Transient transfection of human embryonic kidney (HEK) 293T cells showed that TMEM86b cDNA yielded lysoplasmalogenase activity, and Western blot analyses confirmed the synthesis of TMEM86b protein. The protein was localized in the membrane fractions. The TMEM86b gene was also transformed into Escherichia coli, and its expression was verified by Western blot and activity analyses. Tmem86b is a hydrophobic transmembrane protein of the YhhN family. Northern blot analyses demonstrated that liver expressed the highest level of Tmem86b, which agreed with tissue distribution of activity. Overexpression of TMEM86b in HEK 293T cells resulted in decreased levels of plasmalogens, suggesting that the enzyme may be important in regulating plasmalogen levels in animal cells.
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