scholarly journals Acyl-acyl carrier protein is a donor of fatty acids in the NodA-dependent step in biosynthesis of lipochitin oligosaccharides by rhizobia.

1997 ◽  
Vol 179 (12) ◽  
pp. 4053-4055 ◽  
Author(s):  
T Ritsema ◽  
B J Lugtenberg ◽  
H P Spaink
Keyword(s):  
Fatty Acids ◽  
Acyl Carrier Protein ◽  
Carrier Protein

scholarly journals A universal pocket in Fatty acyl-AMP ligases ensures redirection of fatty acid pool away from Coenzyme A-based activation

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Gajanan Shrikant Patil ◽  
Priyadarshan Kinatukara ◽  
Sudipta Mondal ◽  
Sakshi Shambhavi ◽  
Ketan D Patel ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Binding Sites ◽  
Molecular Basis ◽  
Coenzyme A ◽  
Acyl Carrier Protein ◽  
Fatty Acyl ◽  
Carrier Protein ◽  
Binding Pockets ◽  
Fatty Acid Pool ◽  
Do So

Fatty acyl-AMP ligases (FAALs) channelize fatty acids towards biosynthesis of virulent lipids in mycobacteria and other pharmaceutically or ecologically important polyketides and lipopeptides in other microbes. They do so by bypassing the ubiquitous coenzyme A-dependent activation and rely on the acyl carrier protein-tethered 4'-phosphopantetheine (holo-ACP). The molecular basis of how FAALs strictly reject chemically identical and abundant acceptors like coenzyme A (CoA) and accept holo-ACP unlike other members of the ANL superfamily remains elusive. We show FAALs have plugged the promiscuous canonical CoA-binding pockets and utilize highly selective alternative binding sites. These alternative pockets can distinguish adenosine 3', 5'-bisphosphate-containing CoA from holo-ACP and thus FAALs can distinguish between CoA and holo-ACP. These exclusive features helped identify the omnipresence of FAAL-like proteins and their emergence in plants, fungi, and animals with unconventional domain organisations. The universal distribution of FAALs suggests they are parallelly evolved with FACLs for ensuring a CoA-independent activation and redirection of fatty acids towards lipidic metabolites.

scholarly journals Structures of β-Ketoacyl-Acyl Carrier Protein Synthase I Complexed with Fatty Acids Elucidate its Catalytic Machinery

Structure ◽  
2001 ◽  
Vol 9 (3) ◽  
pp. 233-243 ◽  
Author(s):  
Johan Gotthardt Olsen ◽  
Anders Kadziola ◽  
Penny von Wettstein-Knowles ◽  
Mads Siggaard-Andersen ◽  
Sine Larsen
Keyword(s):  
Fatty Acids ◽  
Acyl Carrier Protein ◽  
Carrier Protein

scholarly journals Molecular basis for the substrate specificity of quorum signal synthases

2017 ◽  
Vol 114 (34) ◽  
pp. 9092-9097 ◽  
Author(s):  
Shi-Hui Dong ◽  
Nicole D. Frane ◽  
Quin H. Christensen ◽  
E. Peter Greenberg ◽  
Rajesh Nagarajan ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Substrate Specificity ◽  
Molecular Basis ◽  
Acyl Carrier Protein ◽  
Acyl Donor ◽  
Carrier Protein ◽  
Homoserine Lactones ◽  
Acyl Homoserine Lactones ◽  
Signal Synthesis ◽  
Enzyme Complexes

In severalProteobacteria, LuxI-type enzymes catalyze the biosynthesis of acyl–homoserine lactones (AHL) signals usingS-adenosyl–l-methionine and either cellular acyl carrier protein (ACP)-coupled fatty acids or CoA–aryl/acyl moieties as progenitors. Little is known about the molecular mechanism of signal biosynthesis, the basis for substrate specificity, or the rationale for donor specificity for any LuxI member. Here, we present several cocrystal structures of BjaI, a CoA-dependent LuxI homolog that represent views of enzyme complexes that exist along the reaction coordinate of signal synthesis. Complementary biophysical, structure–function, and kinetic analysis define the features that facilitate the unusual acyl conjugation withS-adenosylmethionine (SAM). We also identify the determinant that establishes specificity for the acyl donor and identify residues that are critical for acyl/aryl specificity. These results highlight how a prevalent scaffold has evolved to catalyze quorum signal synthesis and provide a framework for the design of small-molecule antagonists of quorum signaling.

scholarly journals Rapid in Vivo Acylation of Acyl Carrier Protein with Exogenous Fatty Acids in Spirodela oligorrhiza

1989 ◽  
Vol 89 (2) ◽  
pp. 707-711 ◽  
Author(s):  
Autar K. Mattoo ◽  
Franklin E. Callahan ◽  
Roshni A. Mehta ◽  
John B. Ohlrogge
Keyword(s):  
Fatty Acids ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Spirodela Oligorrhiza

scholarly journals ACYL-ACYL CARRIER PROTEIN DESATURASE2 and 3 Are Responsible for Making Omega-7 Fatty Acids in the Arabidopsis Aleurone

2016 ◽  
Vol 172 (1) ◽  
pp. 154-162 ◽  
Author(s):  
Fiona M. Bryant ◽  
Olaya Munoz-Azcarate ◽  
Amélie A. Kelly ◽  
Frédéric Beaudoin ◽  
Smita Kurup ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Acyl Carrier Protein ◽  
Carrier Protein

scholarly journals The Two Functional Enoyl-Acyl Carrier Protein Reductases of Enterococcus faecalis Do Not Mediate Triclosan Resistance

mBio ◽  
2013 ◽  
Vol 4 (5) ◽  
Author(s):  
Lei Zhu ◽  
Hongkai Bi ◽  
Jincheng Ma ◽  
Zhe Hu ◽  
Wenbin Zhang ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Enterococcus Faecalis ◽  
Fatty Acid Synthesis ◽  
Acyl Carrier Protein ◽  
Acid Synthesis ◽  
Carrier Protein ◽  
Content Type ◽  
Enoyl Acp Reductase ◽  
Triclosan Resistance

ABSTRACTEnoyl-acyl carrier protein (enoyl-ACP) reductase catalyzes the last step of the elongation cycle in the synthesis of bacterial fatty acids. TheEnterococcus faecalisgenome contains two genes annotated as enoyl-ACP reductases, a FabI-type enoyl-ACP reductase and a FabK-type enoyl-ACP reductase. We report that expression of either of the two proteins restores growth of anEscherichia colifabItemperature-sensitive mutant strain under nonpermissive conditions.In vitroassays demonstrated that both proteins support fatty acid synthesis and are active with substrates of all fatty acid chain lengths. Although expression ofE. faecalis fabKconfers toE. colihigh levels of resistance to the antimicrobial triclosan, deletion offabKfrom theE. faecalisgenome showed that FabK does not play a detectable role in the inherent triclosan resistance ofE. faecalis. Indeed, FabK seems to play only a minor role in modulating fatty acid composition. Strains carrying a deletion offabKgrow normally without fatty acid supplementation, whereasfabIdeletion mutants make only traces of fatty acids and are unsaturated fatty acid auxotrophs.IMPORTANCEThe finding that exogenous fatty acids support growth ofE. faecalisstrains defective in fatty acid synthesis indicates that inhibitors of fatty acid synthesis are ineffective in counteringE. faecalisinfections because host serum fatty acids support growth of the bacterium.

scholarly journals Structure of a Specialized Acyl Carrier Protein Essential for Lipid A Biosynthesis with Very Long-Chain Fatty Acids in Open and Closed Conformations

Biochemistry ◽  
2012 ◽  
Vol 51 (37) ◽  
pp. 7239-7249 ◽  
Author(s):  
Theresa A. Ramelot ◽  
Paolo Rossi ◽  
Farhad Forouhar ◽  
Hsiau-Wei Lee ◽  
Yunhuang Yang ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Lipid A ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Long Chain Fatty Acids ◽  
Lipid A Biosynthesis ◽  
Long Chain ◽  
Chain Fatty Acids

scholarly journals Chlamydia trachomatisScavenges Host Fatty Acids for Phospholipid Synthesis via an Acyl-Acyl Carrier Protein Synthetase

2015 ◽  
Vol 290 (36) ◽  
pp. 22163-22173 ◽  
Author(s):  
Jiangwei Yao ◽  
V. Joshua Dodson ◽  
Matthew W. Frank ◽  
Charles O. Rock
Keyword(s):  
Fatty Acids ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Phospholipid Synthesis

scholarly journals Molecular cloning and characterisation of an acyl carrier protein thioesterase gene (CocoFatB1) expressed in the endosperm of coconut (Cocos nucifera) and its heterologous expression in Nicotiana tabacum to engineer the accumulation of different fatty acids

2014 ◽  
Vol 41 (1) ◽  
pp. 80 ◽  
Author(s):  
Yijun Yuan ◽  
Yinhua Chen ◽  
Shan Yan ◽  
Yuanxue Liang ◽  
Yusheng Zheng ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Amino Acid ◽  
Nicotiana Tabacum ◽  
Acyl Carrier Protein ◽  
Cocos Nucifera ◽  
Chain Elongation ◽  
Carrier Protein ◽  
Medium Chain ◽  
Tobacco Seeds

Coconut (Cocos nucifera L.) contains large amounts of medium chain fatty acids, which mostly recognise acyl-acyl carrier protein (ACP) thioesterases that hydrolyse acyl-ACP into free fatty acids to terminate acyl chain elongation during fatty acid biosynthesis. A full-length cDNA of an acyl-ACP thioesterase, designated CocoFatB1, was isolated from cDNA libraries prepared from coconut endosperm during fruit development. The gene contained an open reading frame of 1254 bp, encoding a 417-amino acid protein. The amino acid sequence of the CocoFatB1 protein showed 100% and 95% sequence similarity to CnFatB1 and oil palm (Elaeis guineensis Jacq.) acyl-ACP thioesterases, respectively. Real-time fluorescent quantitative PCR analysis indicated that the CocoFatB1 transcript was most abundant in the endosperm from 8-month-old coconuts; the leaves and endosperm from 15-month-old coconuts had ~80% and ~10% of this level. The CocoFatB1 coding region was overexpressed in tobacco (Nicotiana tabacum L.) under the control of the seed-specific napin promoter following Agrobacterium tumefaciens-mediated transformation. CocoFatB1 transcript expression varied 20-fold between different transgenic plants, with 21 plants exhibiting detectable levels of CocoFatB1 expression. Analysis of the fatty acid composition of transgenic tobacco seeds showed that the levels of myristic acid (14 : 0), palmitic acid (16 : 0) and stearic acid (18 : 0) were increased by 25%, 34% and 17%, respectively, compared with untransformed plants. These results indicated that CocoFatB1 acts specifically on 14 : 0-ACP, 16 : 0-ACP and 18 : 0-ACP, and can increase medium chain saturated fatty acids. The gene may valuable for engineering fatty acid metabolism in crop improvement programmes.

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