Suicidal dephosphorylation of thiamine pyrophosphate coupled with pyruvate dehydrogenase complex.
Earlier it was noted that purified pyruvate dehydrogenase complex (PDC) produced by "Sigma" usually contains almost saturating amounts of thiamine pyrophosphate (ThPP). In this communication we present the observation that the endogenous ThPP coupled to PDC is dephosphorylated while staying at -10 degrees C, because in the enzyme preparation thiamine monophosphate and un-phosphorylated thiamine appear (HPLC determination). Under the same conditions exogenous ThPP is not dephosphorylated despite contact with the PDC preparation. This may suggest that interactions of some active groups of the enzyme with molecules of endogenous ThPP leads to break-up of the phosphoesters bonds, and destruction of the coenzyme. Decrease of PDC activity during storage is not in proportion with the degree of ThPP dephosphorylation. However the observed instability of PDC activity may be a consequence of the spontaneous process of its coenzyme autodestruction.
Department of Animal Biochemistry, Institute of Biology, University of Bialystok, ul. Swierkowa 20B 15-950 Bialystok, Poland. sstrum@uwb.edu.pl
Slawomir
S
Strumilo
Pawel
P
Dobrzyn
Jan
J
Czerniecki
Adam
A
Tylicki
D000818:Animals; D004356:Drug Storage; D005615:Freezing; D009206:Myocardium / Q000201:enzymology; D011768:Pyruvate Dehydrogenase Complex / Q000378:metabolism* / Q000592:standards*; D013552:Swine; D013833:Thiamine Monophosphate / Q000032:analysis; D013835:Thiamine Pyrophosphate / Q000737:chemistry* / Q000378:metabolism*
D011768:Pyruvate Dehydrogenase Complex; D013833:Thiamine Monophosphate; D013835:Thiamine Pyrophosphate