Literature summary extracted from

Lee, H.J.; Wang, M.; Paschke, R.; Nandy, A.; Ghisla, S.; Kim, J.J.
Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity (1996), Biochemistry, 35, 12412-12420.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.3.8.7	wild-type and E376G/T255E double mutant enzyme and enzyme substrate complexes, vapor diffusion method at 4°C using the sitting drop technique, 0.027 mg enzyme in 140 mM Tris-acetate, pH 7.0, 8% w/v polyethylene glycol 4000, the human enzyme structure is essentially the same as that of the pig enzyme	Homo sapiens

Organism

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

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.3.8.7	wild-type and E376G/T255E double mutant enzyme	Homo sapiens

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
1.3.8.7	a medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein	the catalytic base responsible for the alpha-proton abstraction is E376 in medium-chain acyl-CoA dehydrogenase, while that in long-chain acyl-CoA dehydrogenase is E255	Homo sapiens	a

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Release 2023.1 (January 2023)