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

✍ Scribed by Jan Ignacak; Maria Barbara Stachurska

• Book ID: 117733750
• Publisher: Elsevier Science
• Year: 2003
• Tongue: English
• Weight: 431 KB
• Volume: 134
• Category: Article
• ISSN: 1096-4959
• DOI: 10.1016/s1096-4959(02)00283-x

✦ Synopsis

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.