EC Number   |
Subunits |
Reference |
|---|
   2.3.1.26 | ? |
x * 45000-50000, SDS-PAGE |
486703 |
| 2.3.1.26 | ? |
x * 48000, SDS-PAGE |
736702 |
| 2.3.1.26 | ? |
x * 58000, SDS-PAGE |
486696 |
| 2.3.1.26 | ? |
x * 64000, denaturing electrophoresis conditions |
486699 |
| 2.3.1.26 | ? |
x * 71300, calculated, x * 71000, SDS-PAGE |
660876 |
| 2.3.1.26 | homotetramer |
HisACAT1 |
486710 |
| 2.3.1.26 | homotetramer |
use of chemical cross-linking agent disuccinimidyl suberate causes the formation of material two to four times the size of the monomeric enzyme when added to intact cells expressing either wild-type ACAT1 or mutant ACAT1 C92/333/345/365/387/467/516/528/546A |
486709 |
| 2.3.1.26 | More |
ACAT1 contains two dimerization motifs. The first motif is located near the N-terminus and is not conserved. Deletion of the N-terminal dimerization domain converts ACAT1 to a dimer with full catalytic activity, i.e. ACAT1 is a two-fold dimer. The second dimerization domain, located near the C-terminus, is conserved |
755902 |
| 2.3.1.26 | More |
deleting a dimer-forming motif from the full-length ACAT1 converts the enzyme from a homotetramer to a homodimer that is more catalytically active than the native homotetramer |
486710 |
| 2.3.1.26 | More |
SDS-PAGE: detection of two protein bands with apparent sizes at 50 and 56 kDa, immunoblots: existence of 100 and 200 kDa bands, clarification of these observations needed |
486697 |
