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Purification and characterization of 3-ketoacyl-acyl carrier protein synthase III from spinach. A condensing enzyme utilizing acetyl-coenzyme A to initiate fatty acid synthesis. by R.C. Clough; A.L. Matthis; S.R. Barnum; J.G. Jaworski is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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The 3-ketoacyl-acyl carrier protein (ACP) synthase III from spinach was purified to homogeneity by an eight-step procedure that included an ACP-affinity column. The size of the native enzyme was M(r) = 63,000 based on gel filtration, and its subunit size was M(r) = 40,500 based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, suggesting that 3-ketoacyl-ACP synthase III may be a homodimer. The purified enzyme was highly specific for acetyl-CoA and malonyl-ACP. The Km for acetyl-CoA was 5 microM when assayed in the presence of 10 microM malonyl-CoA. Acetyl-, butyryl-, and hexanoyl-ACP would not substitute for acetyl-CoA as substrates. The specificity for acetyl-CoA suggested that the physiological function of 3-ketoacyl-ACP synthase is to catalyze the initial condensation reaction in fatty acid biosynthesis. The homogeneous 3-ketoacyl-ACP synthase was capable of catalyzing acetyl-CoA:ACP transacylation but at a rate about 90-fold slower than the condensation reaction with malonyl-ACP. The 3-ketoacyl-ACP synthase was inhibited 100% by 5 mM N-ethylmaleimide or 20 mM sodium arsenite.

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Author

R.C. Clough; A.L. Matthis; S.R. Barnum; J.G. Jaworski

Publisher

Elsevier BV

Published

1992

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)