Abstract
A protein rheostat: A strategy for controlling enzyme activity by cleavage of a low-affinity "pseudosubstrate" inhibitor from an autoregulated version of the enzyme (see figure) is described. Peptide-bond cleavage was mediated by conditional protein splicing. The small molecule rapamycin was used to induce intein trans-splicing of the catalytic subunit of cAMP-dependent protein kinase A (PKA).
Original language | English (US) |
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Pages (from-to) | 5189-5192 |
Number of pages | 4 |
Journal | Angewandte Chemie - International Edition |
Volume | 43 |
Issue number | 39 |
DOIs | |
State | Published - Oct 4 2004 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- General Chemistry
- Catalysis
Keywords
- Enzymes
- Inhibitors
- Protein kinase
- Protein splicing