Abstract
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 language | English |
|---|---|
| Pages (from-to) | 305-308 |
| Number of pages | 4 |
| Journal | Biochemical Journal |
| Volume | 266 |
| Issue number | 1 |
| Publication status | Published - 1990 |
| Externally published | Yes |