A report on Cofactor (biochemistry) and Pyruvate decarboxylase

The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.
Mechanism of pyruvate decarboxylation.
A simple [Fe2S2] cluster containing two iron atoms and two sulfur atoms, coordinated by four protein cysteine residues.
The redox reactions of nicotinamide adenine dinucleotide.

Pyruvate decarboxylase depends on cofactors thiamine pyrophosphate (TPP) and magnesium.

- Pyruvate decarboxylase

Another example is thiamine pyrophosphate (TPP), which is tightly bound in transketolase or pyruvate decarboxylase, while it is less tightly bound in pyruvate dehydrogenase.

- Cofactor (biochemistry)
The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.

1 related topic with Alpha

Overall
The "ylide form" of TPP.

Thiamine pyrophosphate

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Thiamine (vitamin B1) derivative which is produced by the enzyme thiamine diphosphokinase.

Thiamine (vitamin B1) derivative which is produced by the enzyme thiamine diphosphokinase.

The "ylide form" of TPP.
TPP Mechanism
The TPP thiazolium ring can be deprotonated at C2 to become an ylid.
A full view of TPP. The arrow indicates the acidic proton.

Thiamine pyrophosphate is a cofactor that is present in all living systems, in which it catalyzes several biochemical reactions.

Pyruvate decarboxylase in ethanol fermentation