CoFactor: Thiamine diphosphate
ThDP catalyses the formation and cleavage of C-S, C-N, C-O and the chemically challenging C-C bonds using the enamine intermediate carbanion. 
Chemical propertiesThiamine diphosphate (ThDP) consists of three parts:
The sequence motif for the ThDP binding site is GDG(X)N and binds the diphosphate group, which is usually coordinated by a Mg2+ ion. The aminopyrimidine ring binds in a hydrophobic pocket, in proximity to an activating invariant GLU residue. Accessibility to the active site is varying and depends on the length of active site loops. 
Thiamine diphosphate metabolism is shared by all forms of life. TPP is involved in energy production, sugar metabolism and other essential pathways .
The deficiency disease of ThDP in humans is called beri-beri.