ArticleBMC structural biology2008
Crystal structures of a purple acid phosphatase, representing different steps of this enzyme's catalytic cycle.
Article in BMC structural biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 95 citations in OpenAlex.
- Analysis and characterization of a novel metallophosphoesterase fromBiochemistry and biophysics reports · 2026Article
- Frontiers in fungal phosphatases: molecular diversity, regulatory mechanisms, analytical methodologies, ecological significance, and prospects for sustainable utilization.Frontiers in bioengineering and biotechnology · 2026Review
- Genome-wide identification, characterization and expression profiling of purple acid phosphatases under variable phosphorus regimes in lentil (Lens culinaris Medik.).BMC plant biology · 2025Article
- Analysis and profiling of the purple acid phosphatase gene family in wheat (Triticum aestivum L.).Protoplasma · 2025Article
- The Fe and Zn cofactor dilemma.Biochimica et biophysica acta. Proteins and proteomics · 2023Review
- Role of the CrcB transporter of Pseudomonas putida in the multi-level stress response elicited by mineral fluoride.Environmental microbiology · 2022Article
- Structure of a cereal purple acid phytase provides new insights to phytate degradation in plants.Plant communications · 2022Article
- Purple acid phosphatases: roles in phosphate utilization and new emerging functions.Plant cell reports · 2022Review
- Principles of fluoride toxicity and the cellular response: a review.Archives of toxicology · 2020Review
- Nitrate and Phosphate Transporters Rescue Fluoride Toxicity in Yeast.Chemical research in toxicology · 2019Article
- Protein replenishment in pitcher fluids of Nepenthes × ventrata revealed by quantitative proteomics (SWATH-MS) informed by transcriptomics.Journal of plant research · 2019Article
- Characterization of the Catalytic Structure of Plant Phytase, Protein Tyrosine Phosphatase-Like Phytase, and Histidine Acid Phytases and Their Biotechnological Applications.Enzyme research · 2018Review
- Haematological evaluation of sodium fluoride toxicity in oryctolagus cunniculus.Toxicology reports · 2017Article
- Catalytic scaffolds for phosphoryl group transfer.Current opinion in structural biology · 2016Review
- Optimal level of purple acid phosphatase5 is required for maintaining complete resistance to Pseudomonas syringae.Frontiers in plant science · 2015Article
- Comparative investigation of the reaction mechanisms of the organophosphate-degrading phosphotriesterases from Agrobacterium radiobacter (OpdA) and Pseudomonas diminuta (OPH).Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Fluoride inhibition of Sporosarcina pasteurii urease: structure and thermodynamics.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Article
- Identification and characterization of an unusual metallo-β-lactamase from Serratia proteamaculans.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
- Purple Acid Phosphatase5 is required for maintaining basal resistance against Pseudomonas syringae in Arabidopsis.BMC plant biology · 2013Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPurple acid phosphatases belong to the family of binuclear metallohydrolases and are involved in a multitude of biological functions, ranging from bacterial killing and bone metabolism in animals to phosphate uptake in plants. Due to its role in bone resorption purple acid phosphatase has evolved into a promising target for the development of anti-osteoporotic chemotherapeutics. The design of specific and potent inhibitors for this enzyme is aided by detailed knowledge of its reaction mechanism. However, despite considerable effort in the last 10 years various aspects of the basic molecular mechanism of action are still not fully understood.
resultsRed kidney bean purple acid phosphatase is a heterovalent enzyme with an Fe(III)Zn(II) center in the active site. Two new structures with bound sulfate (2.4 A) and fluoride (2.2 A) provide insight into the pre-catalytic phase of its reaction cycle and phosphorolysis. The sulfate-bound structure illustrates the significance of an extensive hydrogen bonding network in the second coordination sphere in initial substrate binding and orientation prior to hydrolysis. Importantly, both metal ions are five-coordinate in this structure, with only one nucleophilic mu-hydroxide present in the metal-bridging position. The fluoride-bound structure provides visual support for an activation mechanism for this mu-hydroxide whereby substrate binding induces a shift of this bridging ligand towards the divalent metal ion, thus increasing its nucleophilicity.
conclusionIn combination with kinetic, crystallographic and spectroscopic data these structures of red kidney bean purple acid phosphatase facilitate the proposal of a comprehensive eight-step model for the catalytic mechanism of purple acid phosphatases in general.
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