Active site modification of the β-ketoacyl-ACP synthase FabF3 of Streptomyces coelicolor affects the fatty acid chain length of the CDA lipopeptides

Richard A. Lewis; Laura Nunns; Jenny Thirlway; Kathleen Carroll; Colin P. Smith; Jason Micklefield

doi:10.1039/c0cc03444d

Active site modification of the β-ketoacyl-ACP synthase FabF3 of Streptomyces coelicolor affects the fatty acid chain length of the CDA lipopeptides

Richard A. Lewis, Laura Nunns, Jenny Thirlway, Kathleen Carroll, Colin P. Smith, Jason Micklefield

Research output: Contribution to journal › Article › peer-review

Abstract

Using site directed mutagenesis we altered an active site residue (Phe107) of the enzyme encoded by fabF3 (SCO3248) in the Streptomyces coelicolor gene cluster required for biosynthesis of the calcium dependent antibiotics (CDAs), successfully generating two novel CDA derivatives comprising truncated (C4) lipid side chains and confirming that fabF3 encodes a KAS-II homologue that is involved in determining CDA fatty acid chain length. © 2011 The Royal Society of Chemistry.

Original language	English
Pages (from-to)	1860-1862
Number of pages	3
Journal	Chemical Communications
Volume	47
Issue number	6
Early online date	6 Dec 2010
DOIs	https://doi.org/10.1039/c0cc03444d
Publication status	Published - 14 Feb 2011

Research Beacons, Institutes and Platforms

Manchester Institute of Biotechnology

Access to Document

10.1039/c0cc03444d

Cite this

@article{a2207738d32c4ac6a39251cc8467a7fa,

title = "Active site modification of the β-ketoacyl-ACP synthase FabF3 of Streptomyces coelicolor affects the fatty acid chain length of the CDA lipopeptides",

abstract = "Using site directed mutagenesis we altered an active site residue (Phe107) of the enzyme encoded by fabF3 (SCO3248) in the Streptomyces coelicolor gene cluster required for biosynthesis of the calcium dependent antibiotics (CDAs), successfully generating two novel CDA derivatives comprising truncated (C4) lipid side chains and confirming that fabF3 encodes a KAS-II homologue that is involved in determining CDA fatty acid chain length. {\textcopyright} 2011 The Royal Society of Chemistry.",

author = "Lewis, {Richard A.} and Laura Nunns and Jenny Thirlway and Kathleen Carroll and Smith, {Colin P.} and Jason Micklefield",

note = "BB/C503662, Biotechnology and Biological Sciences Research Council, United KingdomBB/C507210, Biotechnology and Biological Sciences Research Council, United Kingdom",

year = "2011",

month = feb,

day = "14",

doi = "10.1039/c0cc03444d",

language = "English",

volume = "47",

pages = "1860--1862",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "6",

}

TY - JOUR

T1 - Active site modification of the β-ketoacyl-ACP synthase FabF3 of Streptomyces coelicolor affects the fatty acid chain length of the CDA lipopeptides

AU - Lewis, Richard A.

AU - Nunns, Laura

AU - Thirlway, Jenny

AU - Carroll, Kathleen

AU - Smith, Colin P.

AU - Micklefield, Jason

N1 - BB/C503662, Biotechnology and Biological Sciences Research Council, United KingdomBB/C507210, Biotechnology and Biological Sciences Research Council, United Kingdom

PY - 2011/2/14

Y1 - 2011/2/14

N2 - Using site directed mutagenesis we altered an active site residue (Phe107) of the enzyme encoded by fabF3 (SCO3248) in the Streptomyces coelicolor gene cluster required for biosynthesis of the calcium dependent antibiotics (CDAs), successfully generating two novel CDA derivatives comprising truncated (C4) lipid side chains and confirming that fabF3 encodes a KAS-II homologue that is involved in determining CDA fatty acid chain length. © 2011 The Royal Society of Chemistry.

AB - Using site directed mutagenesis we altered an active site residue (Phe107) of the enzyme encoded by fabF3 (SCO3248) in the Streptomyces coelicolor gene cluster required for biosynthesis of the calcium dependent antibiotics (CDAs), successfully generating two novel CDA derivatives comprising truncated (C4) lipid side chains and confirming that fabF3 encodes a KAS-II homologue that is involved in determining CDA fatty acid chain length. © 2011 The Royal Society of Chemistry.

UR - https://doi.org/10.1039/c0cc03444d

U2 - 10.1039/c0cc03444d

DO - 10.1039/c0cc03444d

M3 - Article

C2 - 21135931

SN - 1359-7345

VL - 47

SP - 1860

EP - 1862

JO - Chemical Communications

JF - Chemical Communications

IS - 6

ER -

Active site modification of the β-ketoacyl-ACP synthase FabF3 of Streptomyces coelicolor affects the fatty acid chain length of the CDA lipopeptides

Abstract

Research Beacons, Institutes and Platforms

Access to Document

Other files and links

Fingerprint

Cite this