Mapping of fabC, a locus for the biosynthesis of unsaturated fatty acids in Escherichia coli K12

1973 ◽  
Vol 124 (1) ◽  
pp. 65-67 ◽  
Author(s):  
J. H. F. F. Broekman ◽  
W. P. M. Hoekstra
Keyword(s):  
Escherichia Coli ◽  
Fatty Acids ◽  
Unsaturated Fatty Acids ◽  
Escherichia Coli K12

Studies on the Metabolism of Unsaturated Fatty Acids. VIII. Induction of 2,4-Dienoyl-CoA Reductase in Escherichia coli on the Addition of Unsaturated Fatty Acids1

1982 ◽  
Vol 91 (4) ◽  
pp. 1453-1456 ◽  
Author(s):  
Michinao MIZUGAKI ◽  
Tomoko NISHIMAKI ◽  
Hirotaka YAMAMOTO ◽  
Sumiko NISHIMURA ◽  
Mataichi SAGI ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fatty Acids ◽  
Unsaturated Fatty Acids ◽  
Coa Reductase

scholarly journals Studies on the metabolism of unsaturated fatty acids. IV. N-Ethylmaleimide reducing activity in Escherichia coli K-12.

1981 ◽  
Vol 29 (2) ◽  
pp. 570-573 ◽  
Author(s):  
MICHINAO MIZUGAKI ◽  
TSUNEO UNUMA ◽  
TAKAYUKI SHIRAISHI ◽  
TOMOKO NISHIMAKI ◽  
HIROSHI YAMANAKA
Keyword(s):  
Escherichia Coli ◽  
Fatty Acids ◽  
Unsaturated Fatty Acids ◽  
Reducing Activity ◽  
K 12

scholarly journals Overlapping Repressor Binding Sites Result in Additive Regulation of Escherichia coli FadH by FadR and ArcA

2010 ◽  
Vol 192 (17) ◽  
pp. 4289-4299 ◽  
Author(s):  
Youjun Feng ◽  
John E. Cronan
Keyword(s):  
Escherichia Coli ◽  
Fatty Acids ◽  
Cyclic Amp ◽  
Unsaturated Fatty Acids ◽  
Genetic Regulation ◽  
Receptor Protein ◽  
Anaerobic Conditions ◽  
Mobility Shift ◽  
Long Chain

ABSTRACT Escherichia coli fadH encodes a 2,4-dienoyl reductase that plays an auxiliary role in β-oxidation of certain unsaturated fatty acids. In the 2 decades since its discovery, FadH biochemistry has been studied extensively. However, the genetic regulation of FadH has been explored only partially. Here we report mapping of the fadH promoter and document its complex regulation by three independent regulators, the fatty acid degradation FadR repressor, the oxygen-responsive ArcA-ArcB two-component system, and the cyclic AMP receptor protein-cyclic AMP (CRP-cAMP) complex. Electrophoretic mobility shift assays demonstrated that FadR binds to the fadH promoter region and that this binding can be specifically reversed by long-chain acyl-coenzyme A (CoA) thioesters. In vivo data combining transcriptional lacZ fusion and real-time quantitative PCR (qPCR) analyses indicated that fadH is strongly repressed by FadR, in agreement with induction of fadH by long-chain fatty acids. Inactivation of arcA increased fadH transcription by >3-fold under anaerobic conditions. Moreover, fadH expression was increased 8- to 10-fold under anaerobic conditions upon deletion of both the fadR and the arcA gene, indicating that anaerobic expression is additively repressed by FadR and ArcA-ArcB. Unlike fadM, a newly reported member of the E. coli fad regulon that encodes another auxiliary β-oxidation enzyme, fadH was activated by the CRP-cAMP complex in a manner similar to those of the prototypical fad genes. In the absence of the CRP-cAMP complex, repression of fadH expression by both FadR and ArcA-ArcB was very weak, suggesting a possible interplay with other DNA binding proteins.

scholarly journals Studies on the metabolism of unsaturated fatty acids. VI. Stereochemical studies of the reaction catalyzed by cis-2-enoyl-coenzyme A reductase of Escherichia coli.

1982 ◽  
Vol 30 (6) ◽  
pp. 2155-2160 ◽  
Author(s):  
MICHINAO MIZUGAKI ◽  
TSUNEO UNUMA ◽  
TOMOKO NISHIMAKI ◽  
TAKAYUKI SHIRAISHI ◽  
AKIHIKO KAWAGUCHI ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fatty Acids ◽  
Unsaturated Fatty Acids ◽  
Coenzyme A ◽  
Coenzyme A Reductase

Studies on the Metabolism of Unsaturated Fatty Acids. XII.1 Reaction Catalyzed by 2,4-Dienoyl-CoA Reductase of Escherichia coli

1983 ◽  
Vol 94 (2) ◽  
pp. 409-413 ◽  
Author(s):  
Michinao MIZUGAKI ◽  
Chiharu KIMURA ◽  
Tomoko NISHIMAKI ◽  
Akihiko KAWAGUCHI ◽  
Shigenobu OKUDA ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fatty Acids ◽  
Unsaturated Fatty Acids ◽  
Coa Reductase

Chemical Characterization and Biological Activity of Escherichia coli Lipopolysaccharides

2020 ◽  
Vol 82 (6) ◽  
pp. 35-42
Author(s):  
O.S. Brovarska ◽  
◽  
L.D. Varbanets ◽  
S.V. Kalinichenko ◽  
◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fatty Acids ◽  
Biological Activity ◽  
Unsaturated Fatty Acids ◽  
Large Population ◽  
The Body ◽  
Gram Negative Bacteria ◽  
Double Immunodiffusion ◽  
Gram Negative ◽  
E Coli

Lipopolysaccharides (LPS) are specific components of the cell envelope of gram-negative bacteria, located at the external surface of their outer membrane and performing a number of important physicochemical and biological functions. The widespread in nature are representatives of Enterobacteriaceae family. Among them there are saprotrophic, useful human symbionts, as well as causative agents of acute intestinal infections. The role of saprophytic intestinal microbiota is not limited only to its participation in the digestion process. The endotoxin released as a result of self-renewal of the cell pool of Escherichia coli partially enters the portal blood and performs antigenic stimulation of the macroorganism. In addition, a small amount of endotoxin can also be released by live gram-negative bacteria, which, given the large population of E. coli in the intestine, can create a sufficiently high concentration of endotoxin. Aim. The study of composition and biological activity of lipopolysaccharides of new E. coli strains, found in the human body. Methods. The objects of investigation were strains of Escherichia coli, isolated from healthy patients at the epidemiological center in Kharkiv. Lipopolysaccharides were extracted from dried cells by 45% phenol water solution at 65–68°С by Westphal and Jann method. The amount of carbohydrates was determined by phenol-sulfuric method. Carbohydrate content was determined in accordance to the calibration curve, which was built using glucose as a standard. The content of nucleic acids was determined by Spirin method, protein − by Lowry method. Serological activity of LPS was investigated by double immunodiffusion in agar using the method of Ouchterlony. Results. In all studied E. coli LPS (2884, 2890, 2892), glucose was dominant monosaccharide (40.5, 41.1, 67.3%, respectively). LPS also contained rhamnose (1.8, 22.9, 1.6%, respectively), ribose (3.5, 6.1, 3.6%, respectively) and galactose (4.1, 20.2, 18.3%, respectively). E. coli 2884 LPS also contained arabinose (1.0%) and mannose (44.8%), while E. coli strains 2890 and 2892 LPS contained heptose (9.7 and 7.8%, respectively). Lipid A composition was presented by fatty acids with a carbon chain length from C12 to C18. As the predominant components were 3-hydroxytetradecanoic (39.2–51.3%) as well as tetradecanoic (23.1–28.5%), dodecanoic (8.9–10.9%), hexadecanoic (4.3–7.2%) and octadecanoic (1.8–2.4%) acids. Unsaturated fatty acids: hexadecenoic (2.0–17.9%) and octadecenoic (3.4–4.2%) have been also identified. It was found that octadecanoic and octadecenoic acids were absent in the LPS of 2884 and 2892 strains, respectively. In SDS-PAAG electrophoresis, a bimodal distribution typical for S-forms of LPS was observed. The studied LPS were toxic and pyrogenic. Double immunodiffusion in agar by Ouchterlony revealed that the tested LPS exhibited an antigenic activity in the homologous system. In heterologous system E. coli 2892 LPS had cross reactivity with LPS of E. coli 2890 and М-17. Since the structure of the O-specific polysaccharide (OPS) of E. coli M-17 was established by us earlier, the results of serological reactions make it possible to suggest an analogy of the E. coli 2892 and 2890 OPS structures with that of E. coli М-17 and their belonging to the same serogroup. Conclusions. The study of the composition and biological activity of LPS of new strains of Escherichia coli 2884, 2890 and 2892, isolated from the body of almost healthy patients, expands our knowledge about the biological characteristics of the species.

scholarly journals RESPIRATION AND PROTEIN SYNTHESIS IN ESCHERICHIA COLI MEMBRANE-ENVELOPE FRAGMENTS

1970 ◽  
Vol 44 (2) ◽  
pp. 376-384 ◽  
Author(s):  
Richard W. Hendler ◽  
Amelia H. Burgess ◽  
Raymond Scharff
Keyword(s):  
Escherichia Coli ◽  
Fatty Acids ◽  
Oxygen Uptake ◽  
Unsaturated Fatty Acids ◽  
Nadh Oxidase ◽  
Saturated Fatty Acids ◽  
Oxygen Electrode ◽  
Reduced Form ◽  
E Coli ◽  
Membrane Envelope

Fatty acids inhibited the ability of Escherichia coli membrane-envelope fragments to catalyze the oxidation of succinate and nicotinamide adenine dinucleotide, reduced form (NADH) and also inhibited the response of the Clark oxygen electrode to nonenzymatic oxygen uptake. In all cases, unsaturated fatty acids were much more inhibitory than saturated fatty acids. Albumin afforded complete protection from inhibition in the nonenzymatic oxygen-uptake experiments but only partial protection for the respiratory activities of the membrane fragments. The succinoxidase activity was totally inhibited by bovine serum albumin at concentrations that inhibited succinate dehydrogenase only slightly and NADH oxidase not at all. The E. coli acellular preparation showed no dehydrogenase or oxidase activity for any of the fatty acids under a variety of conditions. These conditions included variations of pH, concentration of fatty acids, and the presence or absence of albumin, CoA, ATP, NAD, cysteine, succinate, and carnitine. It thus appears that E. coli grown in the absence of fatty acid can not use fatty acids as an energy source.

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