ArticleJournal of molecular biology2008
Comparative enzymology in the alkaline phosphatase superfamily to determine the catalytic role of an active-site metal ion.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- Article
- Molecular Basis for Cγ-N Bond Formation by PLP-Dependent Enzyme LolC.Biochemistry · 2024Article
- Copper-flavonoid family of complexes involved in alkaline phosphatase activation.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023Article
- Response regulator PorX coordinates oligonucleotide signalling and gene expression to control the secretion of virulence factors.Nucleic acids research · 2022Article
- TNAP as a therapeutic target for cardiovascular calcification: a discussion of its pleiotropic functions in the body.Cardiovascular research · 2022Review
- N enrichment affects the arbuscular mycorrhizal fungi-mediated relationship between a C4 grass and a legume.Plant physiology · 2021Article
- 2-Benzylidenebenzofuran-3(2RSC advances · 2021Article
- Revealing enzyme functional architecture via high-throughput microfluidic enzyme kinetics.Science (New York, N.Y.) · 2021Article
- Dual-Selective Catalysis in Dephosphorylation Tuned by HfACS central science · 2021Article
- Inorganic Polyphosphates As Storage for and Generator of Metabolic Energy in the Extracellular Matrix.Chemical reviews · 2019Review
- Article
- Comparative studies on the interaction between biogenic polyamines and bovine intestinal alkaline phosphatases: spectroscopic and theoretical approaches.Journal of biological physics · 2019Article
- ProtMiscuity: a database of promiscuous proteins.Database : the journal of biological databases and curation · 2019Article
- 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
- Analysis of Phosphoryl-Transfer Enzymes with QM/MM Free Energy Simulations.Methods in enzymology · 2018Article
- Differential catalytic promiscuity of the alkaline phosphatase superfamily bimetallo core reveals mechanistic features underlying enzyme evolution.The Journal of biological chemistry · 2017Article
- Evolutionary Genomics of Defense Systems in Archaea and Bacteria.Annual review of microbiology · 2017Review
- Repurposing Suzuki Coupling Reagents as a Directed Fragment Library Targeting Serine Hydrolases and Related Enzymes.Journal of medicinal chemistry · 2017Article
- Mechanistic and Evolutionary Insights from Comparative Enzymology of Phosphomonoesterases and Phosphodiesterases across the Alkaline Phosphatase Superfamily.Journal of the American Chemical Society · 2016Article
- Tungstate as a Transition State Analog for Catalysis by Alkaline Phosphatase.Journal of molecular biology · 2016Article
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3 authors.
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Abstract
Mechanistic models for biochemical systems are frequently proposed from structural data. Site-directed mutagenesis can be used to test the importance of proposed functional sites, but these data do not necessarily indicate how these sites contribute to function. In this study, we applied an alternative approach to the catalytic mechanism of alkaline phosphatase (AP), a widely studied prototypical bimetallo enzyme. A third metal ion site in AP has been suggested to provide general base catalysis, but comparison of AP with an evolutionarily related enzyme casts doubt on this model. Removal of this metal site from AP has large differential effects on reactions of cognate and promiscuous substrates, and the results are inconsistent with general base catalysis. Instead, these and additional results suggest that the third metal ion stabilizes the transferred phosphoryl group in the transition state. These results establish a new mechanistic model for this prototypical bimetallo enzyme and demonstrate the power of a comparative approach for probing biochemical function.
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