Modulatory effect of divalent metal cations on the phosphotyrosine activity of the frog liver acid phosphatase.
Frog liver acid phosphatase hydrolyzes phosphotyrosine at acidic pH optimum. Mn2+, Ca2+ and Mg2+ (but not Zn2+) ions modulate this activity by shifting its pH optimum to physiological pH. This effect is not observed when p-nitrophenylphosphate is used as a substrate. Phosphoserine and phosphothreonine are not hydrolyzed under the same conditions.
Szalewicz
A
A
Institute of Biochemistry and Molecular Biology, University of Wrocław, Poland. agata@bf.uni.wroc.pl
Strzelczyk
B
B
Kubicz
A
A
D000135:Acid Phosphatase / Q000378:metabolism*; D000818:Animals; D002413:Cations, Divalent; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D008099:Liver / Q000187:drug effects* / Q000201:enzymology; D008670:Metals / Q000494:pharmacology*; D019000:Phosphotyrosine / Q000378:metabolism*; D011893:Rana esculenta
D002413:Cations, Divalent; D008670:Metals; D019000:Phosphotyrosine; D000135:Acid Phosphatase