^3^1P NMR investigations on free and enzyme bound thiamine pyrophosphate - Flatau, S.; Fischer, G.; Kleinpeter, E.; Schellenberger, A. (Elsevier)
Pyruvate decarylase (PDC) contains thiamine pyrophosphate (TPP) and Mg^2^+ as cofactors. ^3^1P NMR studies with PDC in the presence of added Mn^2^+ reveal the pyrophosphate moiety of TPP to be a nonaccessible area for the external Mn^2^+ and thus proving the Mg-P-complex (taking part in the binding of the coenzyme to the protein) to be a nonaccessible area for the medium. Glyoxylic acid, acting as an inhibitor of PDC by forming a noncleavable bond with the catalytic center of TPP causes a steric immobilization of the coenzyme indicated by a line broadening of the pyrophosphate moiety.
http://dx.doi.org/10.1016/0014-5793(88)80465-4
Keywords: W; V; U