PMID:7559576
| Citation |
Lambalot, RH and Walsh, CT (1995) Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase. J. Biol. Chem. 270:24658-61 |
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| Abstract |
Holo-acyl carrier protein synthase (ACPS) transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to Ser-36 of acyl carrier protein (ACP) in Escherichia coli. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP. We have purified E. coli ACPS to near homogeneity by exploiting the ability to refold ACPS and reconstitute its activity after elution from an apo-ACP affinity column under denaturing conditions. N-terminal sequencing of ACPS allowed us to identify dpj, an essential gene of previously unknown function, as the structural gene for ACPS. We report herein the 70,000-fold purification of wild-type ACPS and the overproduction and initial characterization of recombinant ACPS from E. coli. |
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| Keywords |
Amino Acid Sequence; Base Sequence; Cloning, Molecular; Escherichia coli/enzymology; Molecular Sequence Data; Protein Processing, Post-Translational; Recombinant Proteins/isolation & purification; Transferases (Other Substituted Phosphate Groups)/biosynthesis; Transferases (Other Substituted Phosphate Groups)/genetics; Transferases (Other Substituted Phosphate Groups)/isolation & purification |
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