This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Synonyms: [acp] metabolism, ACP metabolism
|Superclasses:||Activation/Inactivation/Interconversion → Interconversions|
|Biosynthesis → Cofactors, Prosthetic Groups, Electron Carriers Biosynthesis|
Some taxa known to possess this pathway include : Escherichia coli K-12 substr. MG1655
Expected Taxonomic Range:
All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active. The inactive apo-proteins are converted into their active holo-forms by transfer of the 4'-phosphopantetheine moiety of coenzyme A to the side chain hydroxy group of a conserved serine residue in each ACP domain. The activation is catalyzed by EC 22.214.171.124, holo-[acyl-carrier-protein] synthase
Found only in some bacteria, a dedicated enzyme, EC 126.96.36.199, [acyl-carrier-protein] phosphodiesterase, catalyzes the removal of the 4-phosphopantetheinyl moiety from holo-ACP. The enzyme from Escherichia coli has been characterized, and found not to be essential for growth. Its physiological role is still unknown [Thomas05].
Unification Links: EcoCyc:PWY-6012
Joshi03a: Joshi AK, Zhang L, Rangan VS, Smith S (2003). "Cloning, expression, and characterization of a human 4'-phosphopantetheinyl transferase with broad substrate specificity." J Biol Chem 278(35);33142-9. PMID: 12815048
Thomas05: Thomas J, Cronan JE (2005). "The enigmatic acyl carrier protein phosphodiesterase of Escherichia coli: genetic and enzymological characterization." J Biol Chem 280(41);34675-83. PMID: 16107329
Broadwater99: Broadwater JA, Fox BG (1999). "Spinach holo-acyl carrier protein: overproduction and phosphopantetheinylation in Escherichia coli BL21(DE3), in vitro acylation, and enzymatic desaturation of histidine-tagged isoform I." Protein Expr Purif 15(3);314-26. PMID: 10092491
Carreras97: Carreras CW, Gehring AM, Walsh CT, Khosla C (1997). "Utilization of enzymatically phosphopantetheinylated acyl carrier proteins and acetyl-acyl carrier proteins by the actinorhodin polyketide synthase." Biochemistry 36(39);11757-61. PMID: 9305965
Cox97: Cox RJ, Hitchman TS, Byrom KJ, Findlow IS, Tanner JA, Crosby J, Simpson TJ (1997). "Post-translational modification of heterologously expressed Streptomyces type II polyketide synthase acyl carrier proteins." FEBS Lett 405(3);267-72. PMID: 9108302
Cronan84: Cronan JE (1984). "Evidence that incorporation of exogenous fatty acids into the phospholipids of Escherichia coli does not require acyl carrier protein." J Bacteriol 159(2);773-5. PMID: 6378892
De06: De Lay NR, Cronan JE (2006). "A genome rearrangement has orphaned the Escherichia coli K-12 AcpT phosphopantetheinyl transferase from its cognate Escherichia coli O157:H7 substrates." Mol Microbiol 61(1);232-42. PMID: 16824108
Debabov96: Debabov DV, Heaton MP, Zhang Q, Stewart KD, Lambalot RH, Neuhaus FC (1996). "The D-Alanyl carrier protein in Lactobacillus casei: cloning, sequencing, and expression of dltC." J Bacteriol 178(13);3869-76. PMID: 8682792
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Flugel00: Flugel RS, Hwangbo Y, Lambalot RH, Cronan JE, Walsh CT (2000). "Holo-(acyl carrier protein) synthase and phosphopantetheinyl transfer in Escherichia coli." J Biol Chem 2000;275(2);959-68. PMID: 10625633
Gehring97a: Gehring AM, Lambalot RH, Vogel KW, Drueckhammer DG, 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(1);17-24. PMID: 9070424
Hirvas97: Hirvas L, Nurminen M, Helander IM, Vuorio R, Vaara M (1997). "The lipid A biosynthesis deficiency of the Escherichia coli antibiotic-supersensitive mutant LH530 is suppressed by a novel locus, ORF195." Microbiology 143 ( Pt 1);73-81. PMID: 9025280
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