Literature summary for 1.1.1.35 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.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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)

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

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
heart	-	Sus scrofa	-

Substrates and Products (Substrate)

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

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Sus scrofa

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Release 2023.1 (January 2023)