Studies on the mechanism of fatty acid synthesis. XV. Preparation and general properties of beta-ketoacyl acyl carrier protein reductase from Escherichia coli.

Abstract β-ketoacyl acyl carrier protein (ACP) reductase, isolated from extracts of Escherichia coli and purified about 250-fold, shows optimal activity between pH 6.0 and 7.0, within which range the reaction equilibrium almost completely favors formation of the β-hydroxyacyl ACP derivatives. The equilibrium constant for the reaction at pH 7.0 is 3.93 · 10 7 M. The enzyme is specific for TPNH but appears to be nonspecific for the carbon chain length of the β-ketoacyl group. It exhibits marked preference for β-ketoacyl ACP derivatives over CoA derivatives as substrates. The product of the reaction is the D(−) isomer of the β-hydroxyacyl ACP derivative.

• Publication year

  1966

• Venue

  Biochimica et Biophysica Acta

• Publication date

  1966-04-04

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/0005-2760(66)90001-4PMID 4381013
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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