Literature summary extracted from

Holden, H.M.; Banaszak, L.J.; Frieden, C.; McLoughlin, D.J.
Differences in the binding of coenzyme to L-3-hydroxyacyl-Coenzyme A dehydrogenase in the crystalline state and in solution (1981), FEBS Lett., 132, 15-18.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.1.1.35	two dimers of the enzyme in the asymmetric unit of an orthorombic cell, two coenzyme binding sites per dimer	Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
1.1.1.35	(S)-3-hydroxybutyryl-CoA + NAD+	Sus scrofa	-	acetoacetyl-CoA + NADH	-	r

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.1.1.35	Sus scrofa	-	-	-

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
1.1.1.35	heart	-	Sus scrofa	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.1.1.35	(S)-3-hydroxybutyryl-CoA + NAD+	-	Sus scrofa	acetoacetyl-CoA + NADH	-	r

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.1.1.35	NAD+	-	Sus scrofa

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Release 2023.1 (January 2023)