TY - JOUR
T1 - 2,5-Dialkylresorcinol biosynthesis in Pseudomonas aurantiaca
T2 - Novel head-to-head condensation of two fatty acid-derived precursors
AU - Nowak-Thompson, Brian
AU - Hammer, Philip E.
AU - Hill, D. Steven
AU - Stafford, Jill
AU - Torkewitz, Nancy
AU - Gaffney, Thomas D.
AU - Lam, Stephen T.
AU - Molnár, István
AU - Ligon, James M.
PY - 2003/2
Y1 - 2003/2
N2 - 2-Hexyl-5-propylresorcinol is the predominant analog of several dialkylresorcinols produced by Pseudomonas aurantiaca (Pseudomonas fluorescens BL915). We isolated and characterized three biosynthetic genes that encode an acyl carrier protein, a β-ketoacyl-acyl carrier protein synthase III, and a protein of unknown function, all of which collectively allow heterologous production of 2-hexyl-5-propylresorcinol in Escherichia coli. Two regulatory genes exhibiting similarity to members of the AraC family of transcriptional regulators are also present in the identified gene cluster. Based on the deduced functions of the proteins encoded by the gene cluster and the observed incorporation of labeled carbons from octanoic acid into 2-hexyl-5-propylresorcinol, we propose that dialkylresorcinols are derived from medium-chain-length fatty acids by an unusual head-to-head condensation of β-ketoacyl thioester intermediates. Genomic evidence suggests that there is a similar pathway for the biosynthesis of the flexirubin-type pigments in certain bacteria belonging to the order Cytophagales.
AB - 2-Hexyl-5-propylresorcinol is the predominant analog of several dialkylresorcinols produced by Pseudomonas aurantiaca (Pseudomonas fluorescens BL915). We isolated and characterized three biosynthetic genes that encode an acyl carrier protein, a β-ketoacyl-acyl carrier protein synthase III, and a protein of unknown function, all of which collectively allow heterologous production of 2-hexyl-5-propylresorcinol in Escherichia coli. Two regulatory genes exhibiting similarity to members of the AraC family of transcriptional regulators are also present in the identified gene cluster. Based on the deduced functions of the proteins encoded by the gene cluster and the observed incorporation of labeled carbons from octanoic acid into 2-hexyl-5-propylresorcinol, we propose that dialkylresorcinols are derived from medium-chain-length fatty acids by an unusual head-to-head condensation of β-ketoacyl thioester intermediates. Genomic evidence suggests that there is a similar pathway for the biosynthesis of the flexirubin-type pigments in certain bacteria belonging to the order Cytophagales.
UR - http://www.scopus.com/inward/record.url?scp=0037307973&partnerID=8YFLogxK
U2 - 10.1128/JB.185.3.860-869.2003
DO - 10.1128/JB.185.3.860-869.2003
M3 - Article
C2 - 12533461
AN - SCOPUS:0037307973
SN - 0021-9193
VL - 185
SP - 860
EP - 869
JO - Journal of Bacteriology
JF - Journal of Bacteriology
IS - 3
ER -