Open AccessModulatory effect of divalent metal cations on the phosphotyrosine activity of the frog liver acid phosphatase.
Author(s) -
Agata Szalewicz,
Barbara Strzelczyk,
Aleksandra Kubicz
Publication year - 1999
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.1999_4200
Subject(s) - phosphoserine , chemistry , divalent , hydrolysis , substrate (aquarium) , phosphatase , metal ions in aqueous solution , acid phosphatase , biochemistry , metal , inorganic chemistry , serine , enzyme , biology , organic chemistry , ecology
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.