Abstract
With benzyl alcohol as the varied substrate, sorbinil was found to be a competitive inhibitor of aldose reductase, an enzyme implicated in the etiology of secondary diabetic complications. The Kissorbinil and the Vmax/Km (V/K) benzyl alcohol decreased at low pH with a pk of 7.5 and 7.7, respectively. These observations suggest that both sorbinil and benzyl alcohol bind to the same site on the enzyme. Active site inhibition by sorbinil is consistent with non-competitive inhibition patterns of sorbinil with nucleotide coenzyme or aldehyde as the varied substrate in the direction of aldehyde reduction.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 2427-2429 |
| Number of pages | 3 |
| Journal | Biochemical Pharmacology |
| Volume | 44 |
| Issue number | 12 |
| DOIs | |
| State | Published - Dec 15 1992 |
ASJC Scopus subject areas
- Biochemistry
- Pharmacology
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