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Literature summary for 3.6.1.7 extracted from
- Folding and aggregation are selectively influenced by the conformational preferences of the alpha-helices of muscle acylphosphatase (2001), J. Biol. Chem., 276, 37149-37154.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | the native state of the enzyme presents two alpha-helices. Equilibrium and kinetic measurements for folding indicate that only helix-2, spanning residues 55-67, is largely stabilized in the transition state for folding therfore playing a relevant role in this process. The aggregation rate appears to vary only for the variants in which the propensity of the region corresponding to helix-1, spanning residues 22-32, is changed. Mutations that stabilize the first helix slow down the aggregation process while those that destabilize it increase the aggregation rate | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| muscle | - |
Homo sapiens | - |
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Release 2023.1 (January 2023)
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