ArticleJournal of the American Chemical Society2016
Mechanistic and Evolutionary Insights from Comparative Enzymology of Phosphomonoesterases and Phosphodiesterases across the Alkaline Phosphatase Superfamily.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Widespread promiscuous alkaline phosphatases underscore ancient microbial phosphite utilization.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Multifunctionally diverse alkaline phosphatases of Alteromonas drive the phosphorus cycle in the ocean.Nature communications · 2025Article
- Article
- Hydrophilic/Omniphobic Droplet Arrays for High-throughput and Quantitative Enzymology.Analytical chemistry · 2025Article
- Green Biocatalysis of Xylitol Monoferulate:Biotech (Basel (Switzerland)) · 2025Article
- LPS-DephosphorylatingMicroorganisms · 2024Article
- Decoupling of catalysis and transition state analog binding from mutations throughout a phosphatase revealed by high-throughput enzymology.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Second-Shell Residues Contribute to Catalysis by Predominately Preorganizing the Apo State in PafA.Journal of the American Chemical Society · 2023Article
- Response regulator PorX coordinates oligonucleotide signalling and gene expression to control the secretion of virulence factors.Nucleic acids research · 2022Article
- A widely distributed phosphate-insensitive phosphatase presents a route for rapid organophosphorus remineralization in the biosphere.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- High throughput and quantitative enzymology in the genomic era.Current opinion in structural biology · 2021Review
- Enzyme promiscuity in natural environments: alkaline phosphatase in the ocean.The ISME journal · 2021Article
- Revealing enzyme functional architecture via high-throughput microfluidic enzyme kinetics.Science (New York, N.Y.) · 2021Article
- Niche-adaptation in plant-associated Bacteroidetes favours specialisation in organic phosphorus mineralisation.The ISME journal · 2021Article
- Origin of the Phosphoprotein Phosphatase (PPP) sequence family in Bacteria: Critical ancestral sequence changes, radiation patterns and substrate binding features.BBA advances · 2021Article
- The essential inner membrane protein YejM is a metalloenzyme.Scientific reports · 2020Article
- Article
- Substrate structure-activity relationship reveals a limited lipopolysaccharide chemotype range for intestinal alkaline phosphatase.The Journal of biological chemistry · 2019Article
- Evolutionary repurposing of a sulfatase: A new Michaelis complex leads to efficient transition state charge offset.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Theoretical Studies on Catalysis Mechanisms of Serum Paraoxonase 1 and Phosphotriesterase Diisopropyl Fluorophosphatase Suggest the Alteration of Substrate Preference from Paraoxonase to DFP.Molecules (Basel, Switzerland) · 2018Article
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Authors and funding
10 authors.
Funding
Abstract
Naively one might have expected an early division between phosphate monoesterases and diesterases of the alkaline phosphatase (AP) superfamily. On the contrary, prior results and our structural and biochemical analyses of phosphate monoesterase PafA, from Chryseobacterium meningosepticum, indicate similarities to a superfamily phosphate diesterase [Xanthomonas citri nucleotide pyrophosphatase/phosphodiesterase (NPP)] and distinct differences from the three metal ion AP superfamily monoesterase, from Escherichia coli AP (EcAP). We carried out a series of experiments to map out and learn from the differences and similarities between these enzymes. First, we asked why there would be independent instances of monoesterases in the AP superfamily? PafA has a much weaker product inhibition and slightly higher activity relative to EcAP, suggesting that different metabolic evolutionary pressures favored distinct active-site architectures. Next, we addressed the preferential phosphate monoester and diester catalysis of PafA and NPP, respectively. We asked whether the >80% sequence differences throughout these scaffolds provide functional specialization for each enzyme's cognate reaction. In contrast to expectations from this model, PafA and NPP mutants with the common subset of active-site groups embedded in each native scaffold had the same monoesterase:diesterase specificities; thus, the >10
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