Genomes and Genes
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
- 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
- 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. ..
- 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...
- 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. ..
- 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
- 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 ...
- 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. ..
- Nakahigashi K, Inokuchi H. Nucleotide sequence of the fadA and fadB genes from Escherichia coli. Nucleic Acids Res. 1990;18:4937 pubmed
- 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. ..
- 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...
- 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
- 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. ..
- 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.
- 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...
- 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...