PMID:9070424
| Citation |
Gehring, AM, Lambalot, RH, Vogel, KW, Drueckhammer, DG and Walsh, CT (1997) Ability of Streptomyces spp. acyl carrier proteins and coenzyme A analogs to serve as substrates in vitro for E. coli holo-ACP synthase. Chem. Biol. 4:17-24 |
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| Abstract |
The polyketide natural products are assembled by a series of decarboxylation/condensation reactions of simple carboxylic acids catalyzed by polyketide synthase (PKS) complexes. The growing chain is assembled on acyl carrier protein (ACP), an essential component of the PKS. ACP requires posttranslational modification on a conserved serine residue by covalent attachment of a 4'-phosphopantetheine (P-pant) cofactor to yield active holo-ACP. When ACPs of Streptomyces type II aromatic PKS are overproduced in E. coli, however, typically little or no active holo-ACP is produced, and the ACP remains in the inactive apo-form. |
| Links | |
| Keywords |
Acyl Carrier Protein/metabolism; Anti-Bacterial Agents/metabolism; Cloning, Molecular; Coenzyme A/metabolism; DNA Primers; Escherichia coli/enzymology; Molecular Structure; Multienzyme Complexes/metabolism; Pantetheine/analogs & derivatives; Pantetheine/metabolism; Polymerase Chain Reaction; Recombinant Proteins/biosynthesis; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Streptomyces/metabolism; Substrate Specificity; Transferases (Other Substituted Phosphate Groups)/biosynthesis; Transferases (Other Substituted Phosphate Groups)/isolation & purification; Transferases (Other Substituted Phosphate Groups)/metabolism |
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