ArticleThe Journal of biological chemistry2015
From Protease to Decarboxylase: THE MOLECULAR METAMORPHOSIS OF PHOSPHATIDYLSERINE DECARBOXYLASE.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
25 citing papers in PubMed, 39 citations in OpenAlex.
- Molecular remodelling ofJournal of medical microbiology · 2026Article
- Rewiring mitochondrial phosphatidylethanolamine metabolism identifies new and unaccounted trafficking steps.Journal of lipid research · 2026Article
- Rewiring Mitochondrial Phosphatidylethanolamine Metabolism Identifies New and Unaccounted Trafficking Steps.bioRxiv : the preprint server for biology · 2026Article
- Solid-state cultivation-specific agmatine production by Aspergillus oryzae: current understanding and perspectives.Amino acids · 2026Review
- Structural basis for psilocybin biosynthesis.Nature communications · 2025Article
- Identification and enzymatic properties of arginine decarboxylase fromApplied and environmental microbiology · 2024Article
- Phosphatidylserine-exposing extracellular vesicles in body fluids are an innate defence against apoptotic mimicry viral pathogens.Nature microbiology · 2024Article
- Innovations in Antifungal Drug Discovery among Cell Envelope Synthesis Enzymes through Structural Insights.Journal of fungi (Basel, Switzerland) · 2024Review
- RNA sequencing reveals CircRNA expression profiles in chicken embryo fibroblasts infected with velogenic Newcastle disease virus.Frontiers in veterinary science · 2023Article
- The catalytic and structural basis of archaeal glycerophospholipid biosynthesis.Extremophiles : life under extreme conditions · 2022Review
- Article
- Structural insights into phosphatidylethanolamine formation in bacterial membrane biogenesis.Scientific reports · 2021Article
- Dual Regulation of Phosphatidylserine Decarboxylase Expression by Envelope Stress Responses.Frontiers in molecular biosciences · 2021Article
- Proteolytic Control of Lipid Metabolism.ACS chemical biology · 2019Review
- High-throughput screening for phosphatidylserine decarboxylase inhibitors using a distyrylbenzene-bis-aldehyde (DSB-3)-based fluorescence assay.The Journal of biological chemistry · 2019Article
- Article
- Article
- Role of phospholipid synthesis in the development and differentiation of malaria parasites in the blood.The Journal of biological chemistry · 2018Review
- Preparation of Asymmetric Liposomes Using a Phosphatidylserine Decarboxylase.Biophysical journal · 2018Article
- Horizontal gene cluster transfer increased hallucinogenic mushroom diversity.Evolution letters · 2018Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
Abstract
Phosphatidylserine decarboxylase (PSDs) play a central role in the synthesis of phosphatidylethanolamine in numerous species of prokaryotes and eukaryotes. PSDs are unusual decarboxylase containing a pyruvoyl prosthetic group within the active site. The covalently attached pyruvoyl moiety is formed in a concerted reaction when the PSD proenzyme undergoes an endoproteolytic cleavage into a large β-subunit, and a smaller α-subunit, which harbors the prosthetic group at its N terminus. The mechanism of PSD proenzyme cleavage has long been unclear. Using a coupled in vitro transcription/translation system with the soluble Plasmodium knowlesi enzyme (PkPSD), we demonstrate that the post-translational processing is inhibited by the serine protease inhibitor, phenylmethylsulfonyl fluoride. Comparison of PSD sequences across multiple phyla reveals a uniquely conserved aspartic acid within an FFXRX6RX12PXD motif, two uniquely conserved histidine residues within a PXXYHXXHXP motif, and a uniquely conserved serine residue within a GS(S/T) motif, suggesting that PSDs belong to the D-H-S serine protease family. The function of the conserved D-H-S residues was probed using site-directed mutagenesis of PkPSD. The results from these mutagenesis experiments reveal that Asp-139, His-198, and Ser-308 are all essential for endoproteolytic processing of PkPSD, which occurs in cis. In addition, within the GS(S/T) motif found in all PSDs, the Gly-307 residue is also essential, but the Ser/Thr-309 is non-essential. These results define the mechanism whereby PSDs begin their biochemical existence as proteases that execute one autoendoproteolytic cleavage reaction to give rise to a mature PSD harboring a pyruvoyl prosthetic group.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.