EC Number   |
Protein Variants |
Reference |
|---|
    2.3.1.12 | V188A |
ability to be post-translationally lipoylated remains, far-UV CD spectrum differs from wild-type enzyme |
486229 |
| 2.3.1.12 | E182A |
binding of mutant L2 domain to pyruvate dehydrogenase phosphatase isozyme 1 is hindered |
663011 |
| 2.3.1.12 | E182Q |
binding of mutant L2 domain to pyruvate dehydrogenase phosphatase isozyme 1 is hindered |
663011 |
| 2.3.1.12 | V180S/E181L |
binding of mutant L2 domain to pyruvate dehydrogenase phosphatase isozyme 1 is hindered |
663011 |
| 2.3.1.12 | more |
construction of diverse L2 domain mutants, e.g. substitutions of A172, D173, Leu140, Glu162, Glu181, and Glu179 highly reduce binding of L2 domain to pyruvate dehydrogenase phosphatase isozyme 1 |
663011 |
| 2.3.1.12 | more |
deleting the LAT1 gene abolishes life span extension induced by calorie restriction. Overexpressing Lat1 extends life span, and this life span extension is not further increased by calorie restriction. Similar to calorie restriction, life span extension by Lat1 overexpression largely requires mitochondrial respiration. Lat1 overexpression does not require the Sir2 family to extend life span, suggesting that Lat1 mediates a branch of the calorie restriction pathway that functions in parallel to the Sir2 family |
674890 |
| 2.3.1.12 | H602C |
inactive |
736448 |
| 2.3.1.12 | R297A |
mutant is found to have KD 6.8fold higher than that for the wild-type, indicating a possible involvement of this residue in the interaction with human pyruvate dehydrogenase, but not with the C-terminal residue of beta-subunit |
686772 |
| 2.3.1.12 | K276A |
mutant shows negligible binding to human pyruvate dehydrogenase with 86fold higher KD compared to wild-type |
686772 |
| 2.3.1.12 | K96A |
mutation in potential lipoylation site, mutant protein entirely supports the assignment of Lys96 as the site of lipoylation |
720722 |
