EC Number   |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Reference |
|---|
    2.3.1.21 | -999 |
- |
- |
486543 |
| 2.3.1.21 | -999 |
- |
3-dimensional structural model of CPT I active site based on X-ray diffraction analysis data from similar rat enoyl-CoA hydratase |
486309 |
| 2.3.1.21 | -999 |
- |
amino acid composition |
486528 |
| 2.3.1.21 | -999 |
- |
amino acid sequence of peptides |
486565 |
| 2.3.1.21 | -999 |
- |
amino acid sequence, alignment |
486309, 486541 |
| 2.3.1.21 | -999 |
- |
CPT I is composed of different structural segments: 1. a cytosolic N-terminal domain of 46 amino acid residues, 2. 2 transmembranal parts TM1 and TM2, 3. a 27-residue loop between TM1 and 2, 4. a cytosolic catalytic C-terminal domain, amino acid sequences |
486582 |
| 2.3.1.21 | -999 |
- |
enzyme migrates as part of a detergent micelle with MW of 510000 on gel filtration |
486526 |
| 2.3.1.21 | -999 |
- |
mitochondrial enzyme, 86 kDa malonyl-CoA binding protein complexed with CPT and other proteins of the beta-oxidation |
486542 |
| 2.3.1.21 | 20000 |
- |
x * 20000, CPT I and II, SDS-PAGE |
486583 |
| 2.3.1.21 | 30000 |
- |
x * 30000, SDS-PAGE |
736793 |
