Entry M0215 188.8.131.52 pyruvate decarboxylase
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The carbanion of thiamine diphosphate attacks the carbonyl carbon of pyruvate in a nucleophilic addition that results in the cofactor undergoing double bond rearrangement that results in the deprotonation of Glu51B.
Comment: In Zymomonas mobilis it has been suggested that the pyruvate oxygen is protonated through a proton relay involving Tyr290. However, this residue is not present in the yeast enzyme. Therefore, this represents the most likely mechanism. 
Amino acids involved in the reaction step.
Organic Cofactors involved in the reaction step
Metal Cofactors involved in Step 02
||Bonds Changed in Order
||Atom Types Involved
The C-C bond changes from a single to double bond
The C-N bond changes from a single to double bond
The C-C bond changes from a double to single bond
The C-N bond changes from a double to single bond
The C-O bond changes from a double to single bond
View similar reactions in MACiE.