PMID:8805534

Citation	Leesong, M, Henderson, BS, Gillig, JR, Schwab, JM and Smith, JL (1996) Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site. Structure 4:253-64
Abstract	Escherichia coli beta-hydroxydecanoyl thiol ester dehydrase (dehydrase) is essential to the biosynthesis of unsaturated fatty acids, by shunting a 10-carbon intermediate from the saturated fatty acid pathway into the unsaturated fatty acid pathway. Dehydrase catalyzes reactions of dehydration and of double-bond isomerization on 10-carbon thiol esters of acyl carrier protein (ACP). The aim of this work is to elucidate mechanisms for the two enzymatic reactions, which occur in an unusual bifunctional active site, and to understand the specificity of the enzyme for substrates with 10-carbon fatty acyl chains.
Links	PubMed
Keywords	Binding Sites; Crystallization; Cysteamine/analogs & derivatives; Cysteamine/metabolism; Escherichia coli/chemistry; Escherichia coli/enzymology; Models, Molecular; Prephenate Dehydratase/chemistry; Prephenate Dehydratase/metabolism; Protein Conformation; Protein Folding; Protein Structure, Secondary; Recombinant Proteins/chemistry; Substrate Specificity
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