The dual activity of pyruvate kinase type M2 from chromatin extracts of neoplastic cells

Comp Biochem Physiol B Biochem Mol Biol. 2003 Mar;134(3):425-33. doi: 10.1016/s1096-4959(02)00283-x.


Pyruvate kinase type M(2) from Morris hepatoma 7777 tumour cell nuclei and cytosol, in contrast to types L and M(2) from nuclei and cytosol of normal rat liver, shows the histone H(1) kinase activity. Moreover, in the presence of L-cysteine and without ADP it converts 2-phosphoenolpyruvate (PEP) to pyruvate while in the presence of L-arginine or L-histidine does not. L-Cysteine markedly stimulates the activity of histone H(1) kinase transferring a phosphate group from PEP to, as results suggested, the epsilon -amino group of L-lysine of histone H(1). This, L-cysteine which is known to inhibit the activity of pyruvate kinase type M(2) from neoplastic cells transfering a phosphate from PEP to ADP, can act as a control factor champing the direction of enzymatic reaction in cancer cells.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / pharmacology
  • Animals
  • Arginine / pharmacology
  • Cell Fractionation
  • Chromatin / isolation & purification
  • Chromatin / metabolism
  • Cysteine / pharmacology
  • Cytosol / enzymology
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Inhibitors / pharmacology
  • Histidine / pharmacology
  • Isoenzymes / chemistry
  • Isoenzymes / drug effects
  • Isoenzymes / metabolism
  • Liver / enzymology*
  • Liver Neoplasms, Experimental / enzymology*
  • Phosphoenolpyruvate / pharmacology
  • Pyruvate Kinase / chemistry
  • Pyruvate Kinase / drug effects
  • Pyruvate Kinase / metabolism*
  • Rats
  • Rats, Inbred BUF


  • Chromatin
  • Enzyme Inhibitors
  • Isoenzymes
  • Histidine
  • Phosphoenolpyruvate
  • Adenosine Triphosphate
  • Arginine
  • Pyruvate Kinase
  • Cysteine