title: Inhibition of phosphatase activity by positively-charged cyclodextrins.
abstract: [formula: see text] Aminocyclodextrins are known to bind phosphate esters such as phosphotyrosine and p-nitrophenyl phosphate. This paper describes the inhibition of phosphate ester hydrolysis, as catalyzed by lambda-protein phosphatase and acid phosphatase, that is caused by such binding interactions. ROESY studies provide structural information about the cyclodextrin-aryl phosphate complexes. In addition, these experiments are used to generate approximations of the rates of dissociation of the noncovalent complexes.
authors.affiliation: Department of Chemistry, Brown University, Providence, Rhode Island 02912, USA.
authors.forename: M
authors.initials: M
authors.lastname: Ghosh
authors.forename: T C
authors.initials: TC
authors.lastname: Sanders
authors.forename: R
authors.initials: R
authors.lastname: Zhang
authors.forename: C T
authors.initials: CT
authors.lastname: Seto
mesh_terms: D000135:Acid Phosphatase / Q000037:antagonists & inhibitors / Q000737:chemistry; D003505:Cyclodextrins / Q000138:chemical synthesis / Q000737:chemistry*; D004791:Enzyme Inhibitors / Q000138:chemical synthesis / Q000737:chemistry*; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D009596:Nitrophenols / Q000737:chemistry; D009943:Organophosphorus Compounds / Q000737:chemistry; D010744:Phosphoric Monoester Hydrolases / Q000037:antagonists & inhibitors*; D019000:Phosphotyrosine / Q000737:chemistry; D017027:Protein Tyrosine Phosphatases / Q000037:antagonists & inhibitors / Q000737:chemistry; D054623:Receptor-Like Protein Tyrosine Phosphatases, Class 2
chemical_list: D003505:Cyclodextrins; D004791:Enzyme Inhibitors; D009596:Nitrophenols; D009943:Organophosphorus Compounds; D019000:Phosphotyrosine; C008644:nitrophenylphosphate; D000135:Acid Phosphatase; D010744:Phosphoric Monoester Hydrolases; D017027:Protein Tyrosine Phosphatases; D054623:Receptor-Like Protein Tyrosine Phosphatases, Class 2