A specific sucrose phosphatase from plant tissues

Biochem J. 1966 Apr;99(1):102-7. doi: 10.1042/bj0990102.

Abstract

1. A phosphatase that hydrolyses sucrose phosphate (phosphorylated at the 6-position of fructose) was isolated from sugar-cane stem and carrot roots. With partially purified preparations fructose 6-phosphate, glucose 6-phosphate, fructose 1-phosphate, glucose 1-phosphate and fructose 1,6-diphosphate are hydrolysed at between 0 and 2% of the rate for sucrose phosphate. 2. The activity of the enzyme is increased fourfold by the addition of Mg(2+) ions and inhibited by EDTA, fluoride, inorganic phosphate, pyrophosphate, Ca(2+) and Mn(2+) ions. Sucrose (50mm) reduces activity by 60%. 3. The enzyme exhibits maximum activity between pH6.4 and 6.7. The Michaelis constant for sucrose phosphate is between 0.13 and 0.17mm. 4. At least some of the specific phosphatase is associated with particles having the sedimentation properties of mitochondria. 5. A similar phosphatase appears to be present in several other plant species.

MeSH terms

  • Chemical Phenomena
  • Chemistry
  • Enzymes
  • Hexosephosphates
  • Hydrogen-Ion Concentration
  • Phosphoric Monoester Hydrolases / analysis*
  • Plants, Edible / analysis*

Substances

  • Enzymes
  • Hexosephosphates
  • Phosphoric Monoester Hydrolases