Purple acid phosphatase in the walls of tobacco cells

Phytochemistry. 2008 Oct;69(14):2546-51. doi: 10.1016/j.phytochem.2008.07.008. Epub 2008 Aug 31.


Purple acid phosphatase isolated from the walls of tobacco cells appears to be a 220kDa homotetramer composed of 60kDa subunits, which is purple in color and which contains iron as its only metal ion. Although the phosphatase did not require dithiothreitol for activity and was not inhibited by phenylarsine oxide, the enzyme showed a higher catalytic efficiency (k(cat)/K(m)) for phosphotyrosine-containing peptides than for other substrates including p-nitrophenyl-phosphate and ATP. The phosphatase formed as a 120kDa dimer in the cytoplasm and as a 220kDa tetramer in the walls, where Brefeldin A blocked its secretion during wall regeneration. According to our double-immunofluorescence labeling results, the enzyme might be translocated through the Golgi apparatus to the walls at the interphase and to the cell plate during cytokinesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acid Phosphatase / isolation & purification*
  • Acid Phosphatase / metabolism*
  • Cell Wall / metabolism*
  • Cells, Cultured
  • Electrophoresis, Polyacrylamide Gel
  • Glycoproteins / isolation & purification*
  • Glycoproteins / metabolism*
  • Iron / metabolism
  • Molecular Weight
  • Plant Proteins / isolation & purification
  • Plant Proteins / metabolism*
  • Substrate Specificity
  • Tobacco / enzymology*


  • Glycoproteins
  • Plant Proteins
  • Iron
  • purple acid phosphatase
  • Acid Phosphatase