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Folia Microbiologica 1994Proteins with phosphatase activity were produced during the growth of Aspergillus flavus in a phosphate-supplemented liquid synthetic medium. The best carbon and...
Proteins with phosphatase activity were produced during the growth of Aspergillus flavus in a phosphate-supplemented liquid synthetic medium. The best carbon and nitrogen sources for the synthesis of phosphatase were glucose and ammonium sulfate, respectively. The proteins were separated by molecular exclusion and ion exclusion chromatography (IEC) into three components one of which showed phosphatase activity. The molar mass of the enzyme was approximately 62 kDa. The purified enzyme exhibited an optimum activity at pH 4.0 and at 45 degrees C. The activity of the enzyme was stimulated by Ca2+ and Mg2+ but inhibited by fluoride, iodoacetic acid, ethylenediaminetetraacetic acid and 2,4-dinitrophenol, and exhibited an apparent KM of approximately 420 mumol/L.
Topics: Acid Phosphatase; Ammonium Sulfate; Aspergillus flavus; Calcium; Enzyme Inhibitors; Glucose; Hydrogen-Ion Concentration; Kinetics; Magnesium; Molecular Weight; Temperature
PubMed: 8549995
DOI: 10.1007/BF02814065 -
International Journal of Biological... May 2020The effect of putrescine on the dynamics, conformation, and kinetics of acid phosphatase investigated via different experimental and theoretical methods. The...
The effect of putrescine on the dynamics, conformation, and kinetics of acid phosphatase investigated via different experimental and theoretical methods. The Stern-Volmer constants (K) for the acid phosphatase- putrescine compound was obtained at different temperatures. Therefore, putrescine quenched the intensity of the enzyme via the static method. Gibbs free energy displayed which binding process was spontaneous. MD simulation, docking method, and thermodynamic parameters revealed the van der Waals forces and hydrogen bonding that had the specific interaction in unfolding the compound. After putrescine binding, the V amounts of acid phosphatase without changed, and the value of k/K increased. The T the acid phosphatase-putrescine compound was decreased. Presumably because of more surface hydrophilicity and further H-bond formation underlying the putrescine modification. As confirmed by fluorescence spectra and UV-Visible spectroscopy. Circular dichroism (CD) and UV absorption investigations also demonstrated which binding of putrescine to acid phosphatase led to microenvironmental variations around the protein. Therefore, putrescine cause changes in its structure and function. The results, therefore, showed the effect of putrescine was because of its kosmotropic specifications. Molecular dynamics simulation and Molecular docking results further confirmed the results obtained by CD and spectroscopy experiments.
Topics: Acid Phosphatase; Algorithms; Binding Sites; Enzyme Activation; Enzyme Stability; Hydrogen Bonding; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; Kinetics; Models, Theoretical; Molecular Docking Simulation; Molecular Dynamics Simulation; Protein Binding; Putrescine; Spectrum Analysis; Thermodynamics
PubMed: 32045610
DOI: 10.1016/j.ijbiomac.2020.02.057 -
Journal of Enzyme Inhibition and... Dec 2023Acid phosphatases (EC 3.1.3.2) are the enzymes that catalyse transphosphorylation reactions and promotes the hydrolysis of numerous orthophosphate esters in acidic... (Review)
Review
Acid phosphatases (EC 3.1.3.2) are the enzymes that catalyse transphosphorylation reactions and promotes the hydrolysis of numerous orthophosphate esters in acidic media, as a crucial element for the metabolism of phosphate in tissues. Inorganic phosphate (Pi) utilisation and scavenging, as well as the turnover of Pi-rich sources found in plant vacuoles, are major processes in which intracellular and secretory acid phosphatases function. Therefore, a thorough understanding of these enzymes' structural characteristics, specificity, and physiochemical properties is required to comprehend the function of acid phosphatases in plant energy metabolism. Furthermore, acid phosphatases are gaining increasing importance in industrial biotechnology due to their involvement in transphosphorylation processes and their ability to reduce phosphate levels in food products. Hence, this review aims to provide a comprehensive overview of the purification methods employed for isolating acid phosphatases from diverse plant sources, as well as their structural and functional properties. Additionally, the review explores the potential applications of these enzymes in various fields.
Topics: Acid Phosphatase; Hydrolysis; Plants; Phosphates
PubMed: 37985663
DOI: 10.1080/14756366.2023.2282379 -
Journal of Invertebrate Pathology Nov 2009The use of Duddingtonia flagrans, a nematode-trapping fungus, has been investigated as a biological control method against free living larvae of gastrointestinal...
The use of Duddingtonia flagrans, a nematode-trapping fungus, has been investigated as a biological control method against free living larvae of gastrointestinal nematodes of livestock animals. This fungus captures and infects the nematode by cuticle penetration, immobilization and digestion of the internal contents. It has been suggested that this sequence of events occurs by a combination of physical and enzymatical activities. This report characterizes the acid phosphatase activity during the interaction of D. flagrans with the free-living nematode Panagrellus sp. The optimum pH for the hydrolysis of the acid phosphatase substrate p-nitrophenyl phosphate was 2.2, 2.8 and 5.4 from D. flagrans alone and 2.2 and 5.4 for Panagrellus sp alone, fungus-nematode interaction in liquid medium and fungus-nematode interaction in solid medium. Different acid phosphatase activity bands were detected by SDS-PAGE. Maximum acid phosphatase activity of the fungus or nematode alone and of the fungus-nematode interaction occurred within 70min of incubation in the presence of the substrate 4-methylumbelliferyl phosphate. The activity of this enzyme was significantly higher for the fungus-nematode interaction when compared to the organisms alone, indicating a synergistic response. Furthermore, structures appeared in the hyphae after 30min, nematodes were observed adhered after 40min and many were captured by the typical fungus traps after 70min of interaction. The participation of acid phosphatase activity and its importance during the interaction of the fungus with the nematode were discussed.
Topics: Acid Phosphatase; Animals; Ascomycota; Electrophoresis, Polyacrylamide Gel; Hydrogen-Ion Concentration; Kinetics; Rhabditida; Time Factors
PubMed: 19679133
DOI: 10.1016/j.jip.2009.08.003 -
Analytica Chimica Acta Apr 2020We have developed a simple and convenient route to prepare fluorescent carbon dots with dual emission peaks respectively at 470 and 570 nm. The prepared dual-emission...
We have developed a simple and convenient route to prepare fluorescent carbon dots with dual emission peaks respectively at 470 and 570 nm. The prepared dual-emission carbon dots can be used for ratiometric detection of Fe3+ ions in the range from 0 to 50 μmol·L-1 with 0.8 μmol·L-1 detection limit based on the fluorescence quenching at 570 nm. The quenched fluorescence induced by Fe3+ ions could be recovered by pyrophosphate. We further used the carbon dots-Fe3+ ions-pyrophosphate mixed system for ratiometric detection of acid phosphatase in the range from 0.08 to 6.75 μg·mL-1 with 0.01 μg·mL-1 detection limit.
Topics: Acid Phosphatase; Carbon; Diphosphates; Ferric Compounds; Fluorescent Dyes; Ions; Molecular Structure; Particle Size; Quantum Dots; Spectrometry, Fluorescence; Surface Properties
PubMed: 32138914
DOI: 10.1016/j.aca.2020.01.033 -
Journal of Chromatography. B,... Dec 2002Various biochemical markers have been used to assess bone metabolism and to monitor the effects of treatments. Tartrate resistant acid phosphatase (TRAP; EC 3.1.3.2) has... (Review)
Review
Various biochemical markers have been used to assess bone metabolism and to monitor the effects of treatments. Tartrate resistant acid phosphatase (TRAP; EC 3.1.3.2) has often been used to assess bone absorption. Although osteoclasts contain abundant TRAP and they are responsible for bone resorption, the total TRAP activities in the serum measured by colorimetric methods little reflect the bone turnover. TRAP 5 is further separated into 5a and 5b by electrophoresis. Type 5b is considered to be derived from the osteoclast, and therefore attempts are being made to measure exclusively serum TRAP 5b by kinetic methods, immunological methods, and chromatographic methods including ion-exchange and heparin column chromatography.
Topics: Acid Phosphatase; Biomarkers; Bone and Bones; Chromatography, Liquid; Electrophoresis; Humans; Isoenzymes; Tartrate-Resistant Acid Phosphatase
PubMed: 12450668
DOI: 10.1016/s1570-0232(02)00431-2 -
International Microbiology : the... Sep 2014An acid phosphatase activity was detected in the supernatant of Haemophilus parasuis, a Gram-negative pleomorphic bacillus and the causative agent of Glässer's disease...
An acid phosphatase activity was detected in the supernatant of Haemophilus parasuis, a Gram-negative pleomorphic bacillus and the causative agent of Glässer's disease in pigs. To identify the gene responsible for the secreted activity, a genomic library of H. parasuis strain ER-6P was produced in Escherichia coli. Screening of the library allowed identification of two homologs to known phosphatases: PgpB and AphA. PgpB was predicted to be located in the bacterial membrane through six transmembrane domains while AphA was predicted to have a signal peptide. The aphA gene was cloned and expressed in E. coli. Characterization of H. parasuis AphA indicated that this protein belongs to the class B nonspecific acid phosphatases. AphA contained sequence signatures characteristic of this family of phosphatases and its activity was inhibited by EDTA. The optimal pH of recombinant AphA differed from that of the phosphatase activity found in H. parasuis supernatants. In addition, the phosphatase activity from H. parasuis supernatants was not inhibited by EDTA, indicating that H. parasuis AphA does not account for the phosphatase activity observed in the supernatants. Our results demonstrate the presence of a class B acid phosphatase (AphA) in H. parasuis and suggest that the bacterium would also secrete another, as yet unidentified phosphatase.
Topics: Acid Phosphatase; Amino Acid Sequence; Bacterial Proteins; Enzyme Stability; Haemophilus parasuis; Molecular Sequence Data; Sequence Alignment
PubMed: 26419453
DOI: 10.2436/20.1501.01.216 -
European Journal of Biochemistry Jul 1986We have purified secreted acid phosphatase of Schizosaccharomyces pombe. The enzyme is N-glycosylated, the associated carbohydrate accounts for 90% of the total...
We have purified secreted acid phosphatase of Schizosaccharomyces pombe. The enzyme is N-glycosylated, the associated carbohydrate accounts for 90% of the total molecular mass and the protein moiety has a molecular mass of 54 kDa. The deglycosylated enzyme still exhibits enzymatic activity. Using antibodies recognizing the protein moiety of the enzyme we have identified two intracellular precursors of acid phosphatase: an unglycosylated membrane-bound 54-kDa form that accumulates in the presence of tunicamycin and a partially glycosylated 72-kDa form that accumulates mostly in membranes of cells grown in rich medium. We further showed that the conversion of the 54-kDa and 72-kDa forms to partially glycosylated and fully glycosylated acid phosphatase is a regulated process. Growth conditions determine how much of translated 54-kDa acid phosphatase is glycosylated to the 72-kDa form and how much remains unglycosylated in membranes. When cells are grown in a rich medium, 5% of the total acid phosphatase protein remains as unglycosylated enzyme and 8% as partially glycosylated 72-kDa form. In cells grown in the minimal medium, however, all of the 54-kDa and 72-kDa forms of acid phosphatase are rapidly processed to fully glycosylated enzyme. The 72-kDa form and the unglycosylated form of acid phosphatase are not secreted or transported to the plasma membrane.
Topics: Acid Phosphatase; Autoradiography; Carbohydrate Metabolism; Carbohydrates; Cell Membrane; Culture Media; Saccharomycetales; Schizosaccharomyces
PubMed: 3732265
DOI: 10.1111/j.1432-1033.1986.tb09730.x -
Tidsskrift For Den Norske Laegeforening... Jan 1970
Topics: Acid Phosphatase; Humans; Hydrogen-Ion Concentration; Male; Prostatic Neoplasms
PubMed: 5464316
DOI: No ID Found -
Clinical Chemistry May 1995
Topics: Acid Phosphatase; Biomarkers; Bone Resorption; Drug Resistance; Humans; Osteoblasts; Osteoclasts; Tartrates
PubMed: 7729040
DOI: No ID Found