Literature summary for 1.3.8.7 extracted from

Nishina, Y.; Sato, K.; Tamaoki, H.; Setoyama, C.; Miura, R.; Shiga, K.
FT-IR spectroscopic studies on the molecular mechanism for substrate specificity/activation of medium-chain Acyl-CoA dehydrogenase (2009), J. Biochem., 146, 351-357.

Crystallization (Commentary)

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

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

Organism	UniProt	Comment	Textmining
Sus scrofa	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
kidney	-	Sus scrofa	-

Cofactor

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

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Release 2023.1 (January 2023)