Hexosediphosphatase from spinach chloroplasts: purification, crystallization and some properties.
Hexosediphosphatase (D-fructose-1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11) has been isolated, purified, and crystallized, from previously isolated spinach chloroplasts. The effects of various anions, cations, and sulfhydryl compounds were tested, and activation by Mg2+, glycine, HCO3-, and sulfhydryl compounds is described. The purified enzyme is very specific for fructose 1,6-diphosphate and does not attack sedoheptulose-1,7-bisphosphate. The S20 value of the enzyme was 7.7, from which the molecular weight of the enzyme was estimated as 140,000.
El-Badry
A M
AM
Laboratory of Chemical Biodynamics, Lawrence Berkeley Laboratory, University of California, Berkeley, California 94720, USA.
D002736:Chloroplasts / Q000201:enzymology*; D003460:Crystallization; D005288:Ferredoxins / Q000302:isolation & purification / Q000378:metabolism; D006597:Fructose-Bisphosphatase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000378:metabolism; D008970:Molecular Weight; D010084:Oxidation-Reduction; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D018724:Spinacia oleracea / Q000166:cytology / Q000201:enzymology
D005288:Ferredoxins; D010940:Plant Proteins; D006597:Fructose-Bisphosphatase; D008274:Magnesium