EC Number |
Reaction |
Reference |
---|
2.3.1.21 | palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine |
2 independent inhibitory sites |
486572 |
2.3.1.21 | palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine |
active site three-dimensional structure model |
486309 |
2.3.1.21 | palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine |
broad sepcificity to acyl group, over the range C8 to C18 |
- |
2.3.1.21 | palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine |
CPT I acts at 2 distinct sites, a regulatory and an active site |
486572 |
2.3.1.21 | palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine |
flexible active site |
486530 |
2.3.1.21 | palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine |
optimal activity with palmitoyl-CoA |
- |
2.3.1.21 | palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine |
random sequential mechanism |
486523 |
2.3.1.21 | palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine |
rapid-equilibrium random-order mechanism |
486528 |
2.3.1.21 | palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine |
sigmoidal kinetics with both substrates |
486522 |
2.3.1.21 | palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine |
the catalytic triad is composed of Cys305, His473, and Asp454, with Cys305 serving as a probable nucleophile, thus acting as a site for covalent attachment of the acyl molecule and formation of a stable acyl-enzyme intermediate, mechanism |
674520 |