Abstract
o-Aminophenol is cleaved by the intradiol dioxygenase, pyrocatechase, in an extradiol manner to give picolinic acid as the major product. Inhibition of o-aminophenol cleavage with various reagents was comparable to that observed for catechol cleavage, indicating that both reactions are catalyzed by the same enzyme. Though other substrate analogues have been shown to yield some extradiol cleavage products, this is the first case wherein >95% of the products characterized derived solely from the extradiol cleavage of the ring.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 123-129 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 84 |
| Issue number | 1 |
| DOIs | |
| State | Published - Sep 14 1978 |
Bibliographical note
Funding Information:The author wishes to thank Dr, K. Angelides for helpful discussions Research Corporation and NIH Grant GM-25422 for support of this work.