fadB

Summary

Gene Symbol: fadB
Description: fused 3-hydroxybutyryl-CoA epimerase/delta(3)-cis-delta(2)-trans-enoyl-CoA isomerase/enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase
Alias: ECK3838, JW3822, oldB
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Park S, Lee S. Identification and characterization of a new enoyl coenzyme A hydratase involved in biosynthesis of medium-chain-length polyhydroxyalkanoates in recombinant Escherichia coli. J Bacteriol. 2003;185:5391-7 pubmed
    ..pathway of medium-chain-length (MCL) polyhydroxyalkanoates (PHAs) from fatty acids has been established in fadB mutant Escherichia coli strain by expressing the MCL-PHA synthase gene...
  2. DiRusso C, Metzger A, Heimert T. Regulation of transcription of genes required for fatty acid transport and unsaturated fatty acid biosynthesis in Escherichia coli by FadR. Mol Microbiol. 1993;7:311-22 pubmed
    ..The binding affinity of FadR for OA and OL1 or OL2 was lower than that for the single site within fadB (OB) as measured using protein-DNA gel retention assays...
  3. Yang X, Schulz H, Elzinga M, Yang S. Nucleotide sequence of the promoter and fadB gene of the fadBA operon and primary structure of the multifunctional fatty acid oxidation protein from Escherichia coli. Biochemistry. 1991;30:6788-95 pubmed
    ..the large alpha-subunit of the Escherichia coli fatty acid oxidation complex, was determined by sequencing the fadB region of the fadBA operon. The amino-terminal sequence of this protein had been established by Edman degradation...
  4. Binstock J, Schulz H. Fatty acid oxidation complex from Escherichia coli. Methods Enzymol. 1981;71 Pt C:403-11 pubmed
  5. Yang S, He X, Schulz H. Glutamate 139 of the large alpha-subunit is the catalytic base in the dehydration of both D- and L-3-hydroxyacyl-coenzyme A but not in the isomerization of delta 3, delta 2-enoyl-coenzyme A catalyzed by the multienzyme complex of fatty acid oxidation. Biochemistry. 1995;34:6441-7 pubmed
    ..coli multifunctional protein does not function as a catalytic residue in the isomerization reaction.(ABSTRACT TRUNCATED AT 250 WORDS) ..
  6. Pramanik A, Pawar S, Antonian E, Schulz H. Five different enzymatic activities are associated with the multienzyme complex of fatty acid oxidation from Escherichia coli. J Bacteriol. 1979;137:469-73 pubmed
    ..The five component enzymes of the complex were rapidly inactivated by tris(hydroxymethyl)aminomethane, whereas they remained active in the presence of potassium phosphate. ..
  7. Yang S. Location of the fadBA operon on the physical map of Escherichia coli. J Bacteriol. 1991;173:7405-6 pubmed
  8. Nakahigashi K, Inokuchi H. Nucleotide sequence between the fadB gene and the rrnA operon from Escherichia coli. Nucleic Acids Res. 1990;18:6439 pubmed
  9. Yang S, Schulz H. The large subunit of the fatty acid oxidation complex from Escherichia coli is a multifunctional polypeptide. Evidence for the existence of a fatty acid oxidation operon (fad AB) in Escherichia coli. J Biol Chem. 1983;258:9780-5 pubmed
    ..Additionally, this study provides further evidence for the existence of a fatty acid oxidation (fad AB) operon that codes for the multienzyme complex of fatty acid oxidation and that is located at 85 min on the E. coli chromosome. ..

More Information

Publications24

  1. Pawar S, Schulz H. The structure of the multienzyme complex of fatty acid oxidation from Escherichia coli. J Biol Chem. 1981;256:3894-9 pubmed
  2. Iram S, Cronan J. The beta-oxidation systems of Escherichia coli and Salmonella enterica are not functionally equivalent. J Bacteriol. 2006;188:599-608 pubmed
    ..Exchange of homologous genes between the two organisms showed that the S. enterica FadE and FadBA enzymes were responsible for the greater efficiency of beta-oxidation relative to that of E. coli. ..
  3. Snell K, Feng F, Zhong L, Martin D, Madison L. YfcX enables medium-chain-length poly(3-hydroxyalkanoate) formation from fatty acids in recombinant Escherichia coli fadB strains. J Bacteriol. 2002;184:5696-705 pubmed
    ..coli fadB mutant...
  4. He X, Deng H, Yang S. Importance of the gamma-carboxyl group of glutamate-462 of the large alpha-subunit for the catalytic function and the stability of the multienzyme complex of fatty acid oxidation from Escherichia coli. Biochemistry. 1997;36:261-8 pubmed
    ..Additionally, the negative charge of Glu462 increases the thermostability of the multienzyme complex. ..
  5. Sparkowski J, Das A. The nucleotide sequence of greA, a suppressor gene that restores growth of an Escherichia coli RNA polymerase mutant at high temperature. Nucleic Acids Res. 1990;18:6443 pubmed
  6. Spratt S, Black P, Ragozzino M, Nunn W. Cloning, mapping, and expression of genes involved in the fatty acid-degradative multienzyme complex of Escherichia coli. J Bacteriol. 1984;158:535-42 pubmed
    ..Transposon Tn5 insertional mutagenesis of the cloned fadAB genes has demonstrated that both fadA and fadB are transcribed as a single transcriptional unit with the direction of transcription from fadA to fadB ...
  7. Yang S, Elzinga M. Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme A epimerase with an active site in the amino-terminal domain of the multifunctional fatty acid oxidation protein from Escherichia coli. J Biol Chem. 1993;268:6588-92 pubmed
    ..Moreover, the results suggest that the amino-terminal domain of the large alpha-subunit is also involved in the isomerase activity but the key residue(s) required for catalyzing the isomerization is distinct from the crotonase. ..
  8. Nakahigashi K, Inokuchi H. Nucleotide sequence of the fadA and fadB genes from Escherichia coli. Nucleic Acids Res. 1990;18:4937 pubmed
  9. Haller T, Buckel T, Retey J, Gerlt J. Discovering new enzymes and metabolic pathways: conversion of succinate to propionate by Escherichia coli. Biochemistry. 2000;39:4622-9 pubmed
    ..The identification of YgfG as methylmalonyl CoA decarboxylase expands the range of reactions catalyzed by members of the crotonase superfamily. ..
  10. Han M, Lee J, Lee S, Yoo J. Proteome-level responses of Escherichia coli to long-chain fatty acids and use of fatty acid inducible promoter in protein production. J Biomed Biotechnol. 2008;2008:735101 pubmed publisher
    ..of 52 proteins showing altered expression levels with oleic acid presence, 9 proteins including AldA, Cdd, FadA, FadB, FadL, MalE, RbsB, Udp, and YccU were newly synthesized...
  11. He X, Yang S. Glutamate-119 of the large alpha-subunit is the catalytic base in the hydration of 2-trans-enoyl-coenzyme A catalyzed by the multienzyme complex of fatty acid oxidation from Escherichia coli. Biochemistry. 1997;36:11044-9 pubmed
  12. He X, Yang S. Histidine-450 is the catalytic residue of L-3-hydroxyacyl coenzyme A dehydrogenase associated with the large alpha-subunit of the multienzyme complex of fatty acid oxidation from Escherichia coli. Biochemistry. 1996;35:9625-30 pubmed
    ..Taken together, several lines of evidence lead to the conclusion that His450 is the catalytic residue of L-3-hydroxyacyl-CoA dehydrogenase of the E. coli multifunctional fatty acid oxidation protein. ..
  13. Yang S, Li J, He X, Cosloy S, Schulz H. Evidence that the fadB gene of the fadAB operon of Escherichia coli encodes 3-hydroxyacyl-coenzyme A (CoA) epimerase, delta 3-cis-delta 2-trans-enoyl-CoA isomerase, and enoyl-CoA hydratase in addition to 3-hydroxyacyl-CoA dehydrogenase. J Bacteriol. 1988;170:2543-8 pubmed
    ..Chem. 258:9780-9785, 1983), lead to the conclusion that 3-hydroxyacyl-CoA epimerase, delta 3-cis-delta 2-trans-enoyl-CoA isomerase, and enoyl-CoA hydratase in addition to 3-hydroxyacyl-CoA dehydrogenase are encoded by the fadB gene.
  14. DiRusso C. Primary sequence of the Escherichia coli fadBA operon, encoding the fatty acid-oxidizing multienzyme complex, indicates a high degree of homology to eucaryotic enzymes. J Bacteriol. 1990;172:6459-68 pubmed
    ..J. Bacteriol. 137:469-473, 1979). In the present work, the DNA sequence of the genes encoding these two subunits, fadB and fadA, has been determined...
  15. Yang S, Yang X, Healy Louie G, Schulz H, Elzinga M. Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural organization of the fadAB operon. J Biol Chem. 1990;265:10424-9 pubmed
    ..gene for 3-ketoacyl-CoA thiolase, the fadA gene, is located 109 nucleotides 3' to the stop codon (TGA) of the fadB gene that encodes the alpha-subunit, a multifunctional polypeptide...