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Literature summary for 2.3.1.86 extracted from
- Structural basis for substrate delivery by acyl carrier protein in the yeast fatty acid synthase (2007), Science, 316, 288-290.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| structure determined at 3.1 A resolution with its acyl carrier protein stalled at the active site of ketoacyl synthase. The structure shows the direct interaction of acyl carrier protein with one of the key catalytic centers in a multifunctional enzyme and suggest a model for substrate delivery that might apply to the other catalytic domains as well | Saccharomyces cerevisiae |
| structure of the Saccharomyces cerevisiae FAS determined at 3.1 A resolution with its acyl carrier protein stalled at the active site of ketoacyl synthase. The structure of the yeast FAS complex shows the direct interaction of acyl carrier protein with one of the key catalytic centers in a multifunctional enzyme and suggests a model for substrate delivery | Saccharomyces cerevisiae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| FAS | - |
Saccharomyces cerevisiae |
| yeast fatty acid synthase | - |
Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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