Inactivation of pyruvate decarboxylase by 3-hydroxypyruvate

G. Thomas, R. Diefenbach, R. G. Duggleby*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)


Pyruvate decarboxylase from Zymomonas mobilis is inhibited by 3-hydroxypyruvate, which can also act as a poor substrate. While catalysing the decarboxylation of this alternative substrate, the enzyme undergoes a progressive but partial inactivation over several hours. The extent of inactivation depends upon the pH and upon the concentration of 3-hydroxypyruvate. After partial inactivation and removal of unchanged 3-hydroxypyruvate, enzymic activity recovers slowly. We suggest that inactivation results from accumulation of enzyme-bound glycollaldehyde, which is relatively stable, possibly because it is dehydrated to form an acetyl group.

Original languageEnglish
Pages (from-to)305-308
Number of pages4
JournalBiochemical Journal
Issue number1
Publication statusPublished - 1990
Externally publishedYes


Dive into the research topics of 'Inactivation of pyruvate decarboxylase by 3-hydroxypyruvate'. Together they form a unique fingerprint.

Cite this