Literature summary for 5.3.3.14 extracted from

Leesong, M.; Henderson, B.S.; Gillig, J.R.; Schwab, J.M.; Smith, J.L.
Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site (1996), Structure, 4, 253-264.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
free enzyme and modified by inhibitor 3-decynoyl-N-acteylcysteamine	Escherichia coli

Organism

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

Reaction

Reaction	Comment	Organism	Reaction ID
a trans-dec-2-enoyl-[acyl-carrier protein] = a cis-dec-3-enoyl-[acyl-carrier protein]	the reactions of EC 4.2.1.60 and EC 5.3.3.14 are carried out by the same active site carrying a His and a Asp residue in a hydrophobic environment	Escherichia coli	a

Subunits

Subunits	Comment	Organism
dimer	crystallization data	Escherichia coli

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Release 2023.1 (January 2023)