Behavior of Acetyl Groups Combined with Sulfhydryl Groups in Protein

II. Behavior of Acetyl Groups Combined with Sulfhydryl Groups in Yeast Alcohol Dehydrogenase

Abstract

It was found that acetyl groups combined with SH groups in yeast alcohol dehydrogenase (YADH) were easily released and transferred to SH group of coenzyme A (CoA) in contrast with acetyl group bound to SH group of glutathione. Stabilization of thiolester bonds in S-acetyl-YADH was observed upon denaturation of the protein in the presence of urea.
These findings appeared to open new approach to a problem about mechanism of storage and supply of active acetyl groups in living cells.