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Acyl Carrier Protein

X. Acyl Carrier Protein Synthetase
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      Acyl carrier protein holoprotein (holo-ACP) synthetase, an enzyme which transfers 4′-phosphopantetheine from reduced coenzyme A to acyl carrier protein apoprotein (apo-ACP) to form holo-ACP and 3′,5′-adenosine diphosphate, has been shown in Escherichia coli B.
      At 780-fold purification the enzyme is free of apo-ACP, holo-ACP, and ACP hydrolase. The apparent Km value is 4 × 10−7m for apo-ACP and 1.5 × 10−4m for CoA. Dephospho-CoA and oxidized CoA are inactive as substrates. The enzyme requires Mg++ or Mn++ for activity. Both cations give complex saturation curves, with Mg++ showing substrate activation between 10−2 and 10−1m.
      The holo-ACP formed in the synthetase reaction has full coenzymatic activity as measured in the malonyl-CoA-CO2 exchange reaction. Quantitative conversion of apo-ACP to holo-ACP is readily achieved with an excess of synthetase. Thus this enzyme can be utilized in an assay for apo-ACP in biological material.
      The reverse reaction, formation of CoA from holo-ACP and 3′,5′-adenosine diphosphate, has been shown.

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