Literature summary for 5.3.3.14 extracted from

Guerra, D.J.; Browse, J.A.
Escherichia coli beta-hydroxydecanoyl thioester dehydrase reacts with native C10 acyl-acyl-carrier proteins of plant and bacterial origin (1990), Arch. Biochem. Biophys., 280, 336-345.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	multifunctional enzyme, catalyzing in addition reaction of EC 4.2.1.60	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	enzyme activity depends more on acyl chain length than acyl carrier protein structure or origin	Escherichia coli	?	-	?
trans-2-decenoyl-(acyl-carrier protein)	enzyme is equally active with acyl carrier protein derived from Escherichia coli, spinach or a protein A:acyl carrier protein fusion protein. With acyl carrier protein derived from Escherichia coli or from spinach, equilibrium results in equal amounts of trans-3- or cis-2-decenoyl-(acyl-carrier-protein), regardless of the initial substrate. With the fusion protein, yield is about 17% cis-3- and 49% trans-2-decenoyl-(acyl-carrier-protein)	Escherichia coli	cis-3-decenoyl-(acyl-carrier protein)	-	r
trans-2-decenoyl-N-acetylcysteamine	-	Escherichia coli	cis-3-decenoyl-N-acetylcysteamine	-	r

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Release 2023.1 (January 2023)