Aldehyde Reductase: The Role of C-Terminal Residues in Defining Substrate and Cofactor Specificities
The only major structural difference between aldehyde reductase, a primarily NADPH-dependent aldo–keto reductase, and aldose reductase, a dually coenzyme-specific (NADPH/NADH) member of the same superfamily, is an additional eight amino acid residues in the substrate/inhibitor binding site (C-termin...
Gespeichert in:
Veröffentlicht in: | Archives of biochemistry and biophysics 1998-07, Vol.355 (2), p.137-144 |
---|---|
Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
Zusammenfassung: | The only major structural difference between aldehyde reductase, a primarily NADPH-dependent aldo–keto reductase, and aldose reductase, a dually coenzyme-specific (NADPH/NADH) member of the same superfamily, is an additional eight amino acid residues in the substrate/inhibitor binding site (C-terminal region) of aldehyde reductase. On the premise that this segment defines the substrate specificity of the enzyme, a mutant of aldehyde reductase lacking residues 306–313 was constructed. In contrast to wild-type enzyme, the mutant enzyme reduced a narrower range of aldehydes and the new substrate specificity was not similar to aldose reductase as might have been predicted. A major change in coenzyme specificity was observed, however, the mutant enzyme being distinctly NADH preferring(Km, NADH= 35 μM, compared to |
---|---|
ISSN: | 0003-9861 1096-0384 |
DOI: | 10.1006/abbi.1998.0721 |