scholarly journals Studies on the metabolism of unsaturated fatty acids. I. Synthesis and identification of 6-hydroxydodec-3-cis-enoic acid, the final metabolite of ricinoleic acid by Escherichia coli K-12.

1978 ◽  
Vol 26 (8) ◽  
pp. 2417-2421 ◽  
Author(s):  
MICHINAO MIZUGAKI ◽  
HARU FUKUYAMA ◽  
TAKAO SAKAMOTO ◽  
HIROSHI YAMANAKA
Keyword(s):  
Escherichia Coli ◽  
Fatty Acids ◽  
Ricinoleic Acid ◽  
Unsaturated Fatty Acids ◽  
Enoic Acid ◽  
K 12

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

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 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.

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