Crystallization (Comment) | Organism |
---|---|
FT-IR spectroscopic studies. The hydrogen-bond enthalpy change responsible for the polarization on the transfer of the substrate from aqueous solution to the active site of enzyme is estimated to be 15 kcal/mol. The 1626 per cm band is noticeably weakened in the case of acyl-CoA with acyl chains longer than C12 which are poor substrates, suggesting that C(1) =O is likely to exist in multiple orientations in the active-site cavity, whence the band becomes obscured. A band identical to that of bound C8-CoA is observed in the case of C4-CoA which is a poor substrate, indicating the strong hydrogen bond at C(1)-O | Sus scrofa |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sus scrofa | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
kidney | - |
Sus scrofa | - |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | investigation on the interaction of acyl-CoA with medium-chain acyl-CoA dehydrogenases reconstituted with artificial FADs such as 8-CN-, 7,8-Cl2-, 8-Cl-, 8-OCH3- and 8-NH2-FAD. 8-NH2-FAD-MCAD does not oxidize acyl-CoA, but the wavelength of the absorption maximum of the flavin is altered by acyl-CoAs binding | Sus scrofa |