Medium-chain fatty acid biosynthesis and utilization in Brassica napus plants expressing lauroyl-acyl carrier protein thioesterase

Planta ◽  
1996 ◽  
Vol 198 (1) ◽  
Author(s):  
VictoriaS. Eccleston ◽  
AnnM. Cranmer ◽  
ToniA. Voelker ◽  
JohnB. Ohlrogge
Keyword(s):  
Fatty Acid ◽  
Brassica Napus ◽  
Fatty Acid Biosynthesis ◽  
Acyl Carrier Protein ◽  
Chain Fatty Acid ◽  
Medium Chain Fatty Acid ◽  
Carrier Protein ◽  
Acid Biosynthesis ◽  
Medium Chain

scholarly journals β-Ketoacyl-Acyl Carrier Protein Synthase III (FabH) Is a Determining Factor in Branched-Chain Fatty Acid Biosynthesis

2000 ◽  
Vol 182 (2) ◽  
pp. 365-370 ◽  
Author(s):  
Keum-Hwa Choi ◽  
Richard J. Heath ◽  
Charles O. Rock
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Fatty Acid Biosynthesis ◽  
Acyl Carrier Protein ◽  
Chain Fatty Acid ◽  
Carrier Protein ◽  
Acid Biosynthesis ◽  
Biochemical Basis ◽  
E Coli ◽  
Branched Chain

ABSTRACT A universal set of genes encodes the components of the dissociated, type II, fatty acid synthase system that is responsible for producing the multitude of fatty acid structures found in bacterial membranes. We examined the biochemical basis for the production of branched-chain fatty acids by gram-positive bacteria. Two genes that were predicted to encode homologs of the β-ketoacyl-acyl carrier protein synthase III of Escherichia coli (eFabH) were identified in theBacillus subtilis genome. Their protein products were expressed, purified, and biochemically characterized. Both B. subtilis FabH homologs, bFabH1 and bFabH2, carried out the initial condensation reaction of fatty acid biosynthesis with acetyl-coenzyme A (acetyl-CoA) as a primer, although they possessed lower specific activities than eFabH. bFabH1 and bFabH2 also utilized iso- and anteiso-branched-chain acyl-CoA primers as substrates. eFabH was not able to accept these CoA thioesters. Reconstitution of a complete round of fatty acid synthesis in vitro with purified E. coli proteins showed that eFabH was the only E. colienzyme incapable of using branched-chain substrates. Expression of either bFabH1 or bFabH2 in E. coli resulted in the appearance of a branched-chain 17-carbon fatty acid. Thus, the substrate specificity of FabH is an important determinant of branched-chain fatty acid production.

scholarly journals Condensing enzymes fromCuphea wrightiiassociated with medium chain fatty acid biosynthesis

1998 ◽  
Vol 13 (5) ◽  
pp. 611-620 ◽  
Author(s):  
Mary B. Slabaugh ◽  
Jeffrey M. Leonard ◽  
Steven J. Knapp
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Biosynthesis ◽  
Chain Fatty Acid ◽  
Medium Chain Fatty Acid ◽  
Acid Biosynthesis ◽  
Medium Chain

β-Ketoacyl-acyl carrier protein synthase IV: a key enzyme for regulation of medium-chain fatty acid synthesis in Cuphea lanceolata seeds

Planta ◽  
2002 ◽  
Vol 215 (5) ◽  
pp. 847-854 ◽  
Author(s):  
Burkhardt Schütt ◽  
Amine Abbadi ◽  
Brigitte Loddenkötter ◽  
Monika Brummel ◽  
Friedrich Spener
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Acyl Carrier Protein ◽  
Acid Synthesis ◽  
Chain Fatty Acid ◽  
Medium Chain Fatty Acid ◽  
Carrier Protein ◽  
Medium Chain ◽  
Key Enzyme ◽  
Cuphea Lanceolata

scholarly journals Characterization of β-Ketoacyl-Acyl Carrier Protein Synthase III from Streptomyces glaucescens and Its Role in Initiation of Fatty Acid Biosynthesis

1998 ◽  
Vol 180 (17) ◽  
pp. 4481-4486 ◽  
Author(s):  
Lei Han ◽  
Sandra Lobo ◽  
Kevin A. Reynolds
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Biosynthesis ◽  
Acyl Carrier Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Chain Fatty Acid ◽  
Carrier Protein ◽  
Acid Biosynthesis ◽  
Streptomyces Glaucescens

ABSTRACT The Streptomyces glaucescens fabH gene, encoding β-ketoacyl-acyl carrier protein (β-ketoacyl-ACP) synthase (KAS) III (FabH), was overexpressed in Escherichia coli, and the resulting gene product was purified to homogeneity by metal chelate chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of the purified protein revealed anM r of 37,000, while gel filtration analysis determined a native M r of 72,000 ± 3,000 (mean ± standard deviation), indicating that the enzyme is homodimeric. The purified recombinant protein demonstrated both KAS activity and acyl coenzyme A (acyl-CoA):ACP transacylase (ACAT) activity in a 1:0.12 ratio. The KAS and ACAT activities were both sensitive to thiolactomycin inhibition. The KAS activity of the protein demonstrated a Km value of 3.66 μM for the malonyl-ACP substrate and an unusual broad specificity for acyl-CoA substrates, with Km values of 2.4 μM for acetyl-CoA, 0.71 μM for butyryl-CoA, and 0.41 μM for isobutyryl-CoA. These data suggest that the S. glaucescensFabH is responsible for initiating both straight- and branched-chain fatty acid biosynthesis in Streptomyces and that the ratio of the various fatty acids produced by this organism will be dictated by the ratios of the various acyl-CoA substrates that can react with FabH. Results from a series of in vivo directed biosynthetic experiments in which the ratio of these acyl-CoA substrates was varied are consistent with this hypothesis. An additional set of in vivo experiments using thiolactomycin provides support for the role of FabH and further suggests that a FabH-independent pathway for straight-chain fatty acid biosynthesis operates in S. glaucescens.

scholarly journals Metabolic engineering of medium-chain fatty acid biosynthesis in Nicotiana benthamiana plant leaf lipids

2015 ◽  
Vol 6 ◽  
Author(s):  
Kyle B. Reynolds ◽  
Matthew C. Taylor ◽  
Xue-Rong Zhou ◽  
Thomas Vanhercke ◽  
Craig C. Wood ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Metabolic Engineering ◽  
Nicotiana Benthamiana ◽  
Fatty Acid Biosynthesis ◽  
Chain Fatty Acid ◽  
Benthamiana Plant ◽  
Medium Chain Fatty Acid ◽  
Acid Biosynthesis ◽  
Plant Leaf ◽  
Medium Chain
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