Anion and divalent cation activation of phosphoglycolate phosphatase from leaves.
Phosphoglycolate (P-glycolate) phosphatase was purified 223-fold from spinach leaves by (NH4)2SO4 fractionation, DEAE-cellulose chromatography, and Sephadex G-200 chromatography. The partially purified enzyme had a broad pH optimum between 5.6 and 8.0 and was specific for the hydrolysis of P-glycolate with a Km (P-glycolate) of 26 microM. The enzyme was activated by divalent cations including Mg2+, Co2+, Mn2+, and Zn2+, and by anions including Cl-, Br-, NO-3, and HCOO-. Neither anions nor divalent cations activated the enzyme without the other. The P-glycolate phosphatase activities from tobacco leaves or the green algae, Chlamydomonas reinhardtii, also required Mg2+ and were activated by chloride. In addition, the enzyme was allosterically inhibited by ribose 5-phosphate. The activation of P-glycolate phosphatase by both anions and divalent cations and the inhibition by ribose 5-phosphate may be involved in the in vivo regulation of P-glycolate phosphatase activity.
D000838:Anions; D002021:Buffers; D002413:Cations, Divalent; D004789:Enzyme Activation / Q000187:drug effects; D006016:Glycolates / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D008278:Magnesium Sulfate / Q000494:pharmacology*; D010744:Phosphoric Monoester Hydrolases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D010944:Plants / Q000201:enzymology*; D011189:Potassium Chloride / Q000494:pharmacology*; D012267:Ribosemonophosphates / Q000494:pharmacology
D000838:Anions; D002021:Buffers; D002413:Cations, Divalent; D006016:Glycolates; D012267:Ribosemonophosphates; C031626:ribose-5-phosphate; D011189:Potassium Chloride; D008278:Magnesium Sulfate; C022408:phosphoglycolate phosphatase; D010744:Phosphoric Monoester Hydrolases; C013193:phosphoglycolate