Cofactor designing in functional analysis of thiamin diphosphate enzymes.

@article{Schellenberger1997CofactorDI,
  title={Cofactor designing in functional analysis of thiamin diphosphate enzymes.},
  author={Alfred Schellenberger and Gerhard Dr Huebner and Holger Neef},
  journal={Methods in enzymology},
  year={1997},
  volume={279},
  pages={
          131-46
        }
}
Publisher Summary Thiamin diphosphate (ThDP) has evolved as a cofactor of enzymes catalyzing the splitting and resynthesis of C–C bonds. It reacts exclusively with substrates of the general structure R–CO–X, where X as a cationic leaving group (CO 2 or R–CHO) is replaced by another positively charged residue (Y). ThDP enzymes are pyruvate decarboxylase (PDC) with Y = H - , transketolases (TK) and acetolactate synthase (ALS), with carbonyl compounds as Y, or the α -oxoacid dehydrogenase… CONTINUE READING