Abstract
Structure-prediction and hydrophobic-cluster analysis of several starch hydrolases and related enzymes indicated the organization of eleven domain types. Most enzymes possess a catalytic (β/α)8-barrel and a smaller C-terminal domain as seen in crystal structures of α-amylase and cyclodextrin glucanotransferase. Some also have a starch-granule-binding domain. Enzymes breaking or forming endo-α-1,6 linkages contain domains N-terminal to the (β/α)8-barrel.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 51-55 |
| Number of pages | 5 |
| Journal | Biochemical Journal |
| Volume | 280 |
| Issue number | 1 |
| DOIs | |
| State | Published - 1991 |
| Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology