Literature summary extracted from

Bonito, C.A.; Leandro, P.; Ventura, F.V.; Guedes, R.C.
Insights into medium-chain acyl-CoA dehydrogenase structure by molecular dynamics simulations (2016), Chem. Biol. Drug Des., 88, 281-292 .

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.3.8.7	molecular dynamics simulation and comparison between the porcine MCAD and human MCAD structures. Both proteins are essentially similar	Homo sapiens
1.3.8.7	molecular dynamics simulation and comparison between the porcine MCAD and human MCAD structures. Both proteins are essentially similar	Sus scrofa

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.3.8.7	Homo sapiens	P11310	-	-
1.3.8.7	Sus scrofa	P41367	-	-

Synonyms

EC Number	Synonyms	Comment	Organism
1.3.8.7	ACADM	-	Homo sapiens
1.3.8.7	ACADM	-	Sus scrofa

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.3.8.7	FAD	FAD has an important structural role on the tetramer stability and also in maintaining the volume of the enzyme catalytic pockets. The presence of substrate changes the dynamics of the catalytic pockets and increases FAD affinity	Homo sapiens
1.3.8.7	FAD	FAD has an important structural role on the tetramer stability and also in maintaining the volume of the enzyme catalytic pockets. The presence of substrate changes the dynamics of the catalytic pockets and increases FAD affinity	Sus scrofa

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)