Inhibition of phosphatase activity by positively-charged cyclodextrins.
[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.
Ghosh
M
M
Department of Chemistry, Brown University, Providence, Rhode Island 02912, USA.
Sanders
T C
TC
Zhang
R
R
Seto
C T
CT
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
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