Genomes and Genes
Gene Symbol: gltA
Description: citrate synthase
Alias: ECK0709, JW0710, gluT, icdB
Species: Escherichia coli str. K-12 substr. MG1655
- De Maeseneire S, De Mey M, Vandedrinck S, Vandamme E. Metabolic characterisation of E. coli citrate synthase and phosphoenolpyruvate carboxylase mutants in aerobic cultures. Biotechnol Lett. 2006;28:1945-53 pubmed..Here we examine if over-expression of citrate synthase (gltA) or phosphoenolpyruvate carboxylase (ppc) can eliminate acetate production...
- Wade J, Struhl K. Association of RNA polymerase with transcribed regions in Escherichia coli. Proc Natl Acad Sci U S A. 2004;101:17777-82 pubmed..These observations suggest that in vivo association of sigma(70) and NusA with elongating RNAP is regulated by growth conditions. ..
- Hull E, Spencer M, Wood D, Guest J. Nucleotide sequence of the promoter region of the citrate synthase gene (gltA) of Escherichia coli. FEBS Lett. 1983;156:366-70 pubmedThe gltA gene, specifying the citrate synthase (EC 4.1.3...
- Pereira D, Donald L, Hosfield D, Duckworth H. Active site mutants of Escherichia coli citrate synthase. Effects of mutations on catalytic and allosteric properties. J Biol Chem. 1994;269:412-7 pubmed..The histidine 264 mutant appears to be shifted toward R state and shows weaker binding of the allosteric inhibitor, NADH; thus this mutation also affects the allosteric site, 25-30 A away. ..
- Man W, Li Y, O Connor C, Wilton D. The binding of propionyl-CoA and carboxymethyl-CoA to Escherichia coli citrate synthase. Biochim Biophys Acta. 1995;1250:69-75 pubmed..coli enzyme is more restricted as compared with the enzyme from pig heart and, in the case of propionyl-CoA, this restriction prevents the formation of a catalytically productive enzyme-substrate complex. ..
- Else A, Danson M, Weitzman P. Models of proteolysis of oligomeric enzymes and their applications to the trypsinolysis of citrate synthases. Biochem J. 1988;254:437-42 pubmed..Palmitoyl-CoA is not required for the trypsinolysis of the other citrate synthases, and high concentrations of this metabolite do not affect the correlation of proteolysis with inactivation of these enzymes. ..
- Anderson D, Duckworth H. In vitro mutagenesis of Escherichia coli citrate synthase to clarify the locations of ligand binding sites. J Biol Chem. 1988;263:2163-9 pubmed..The mutant protein was inactive, and acetyl-CoA did not bind to the active site but still inhibited NADH binding. Thus acetyl-CoA can interact with both the allosteric and the active sites of this enzyme. ..
- Wilde R, Guest J. Transcript analysis of the citrate synthase and succinate dehydrogenase genes of Escherichia coli K12. J Gen Microbiol. 1986;132:3239-51 pubmedA transcript analysis of the citrate synthase and succinate dehydrogenase genes (gltA-sdhCDAB) of Escherichia coli was done by nuclease S1 mapping...
- Donald L, Crane B, Anderson D, Duckworth H. The role of cysteine 206 in allosteric inhibition of Escherichia coli citrate synthase. Studies by chemical modification, site-directed mutagenesis, and 19F NMR. J Biol Chem. 1991;266:20709-13 pubmed..Consistent with this explanation is the finding that Cys-206 reacts more quickly with Ellman's reagent in the presence of KCl, and that this rate is faster yet in the E207A mutant. ..
- Walsh K, Koshland D. Characterization of rate-controlling steps in vivo by use of an adjustable expression vector. Proc Natl Acad Sci U S A. 1985;82:3577-81 pubmed..Furthermore, recombinant DNA technology can be used to alter rate-controlling steps in biological pathways and elucidate the regulatory properties of metabolic systems. ..
- Stokell D, Donald L, Maurus R, Nguyen N, Sadler G, Choudhary K, et al. Probing the roles of key residues in the unique regulatory NADH binding site of type II citrate synthase of Escherichia coli. J Biol Chem. 2003;278:35435-43 pubmed..We argue that these two regions are elements in the path of communication between the NADH binding sites and the active sites and are centrally involved in the regulatory conformational change in E. coli citrate synthase. ..
- Maurus R, Nguyen N, Stokell D, Ayed A, Hultin P, Duckworth H, et al. Insights into the evolution of allosteric properties. The NADH binding site of hexameric type II citrate synthases. Biochemistry. 2003;42:5555-65 pubmed
- Nguyen N, Maurus R, Stokell D, Ayed A, Duckworth H, Brayer G. Comparative analysis of folding and substrate binding sites between regulated hexameric type II citrate synthases and unregulated dimeric type I enzymes. Biochemistry. 2001;40:13177-87 pubmed
- Choudhary K, Spicer V, Donald L, Duckworth H, Ens W, Loewen P, et al. Method for estimating the isotopic distributions of metabolically labeled proteins by MALDI-TOFMS: application to NMR samples. Anal Chem. 2006;78:5419-23 pubmed
- Echtenkamp P, Wilson D, Shuler M. Cell cycle progression in Escherichia coli B/r affects transcription of certain genes: Implications for synthetic genome design. Biotechnol Bioeng. 2009;102:902-9 pubmed publisher..In conclusion, gene position, with regard to the C period, and gene function are important factors to incorporate into design criteria for synthetic bacterial genomes. ..
- Rompf A, Schmid R, Jahn D. Changes in protein synthesis as a consequence of heme depletion in Escherichia coli. Curr Microbiol. 1998;37:226-30 pubmed..As a consequence of heme deficiency, the induction of tryptophanase (trpA), citrate synthase (gltA), and aldehyde dehydrogenase (aldA) and the repression of enolase (eno) and phosphoglycerate kinase (pgk) were ..
- Chattopadhyay M, Kern R, Mistou M, Dandekar A, Uratsu S, Richarme G. The chemical chaperone proline relieves the thermosensitivity of a dnaK deletion mutant at 42 degrees C. J Bacteriol. 2004;186:8149-52 pubmed
- Swim H, Krampitz L. Acetic acid oxidation by Escherichia coli; evidence for the occurrence of a tricarboxylic acid cycle. J Bacteriol. 1954;67:419-25 pubmed
- Oden K, DeVeaux L, Vibat C, Cronan J, Gennis R. Genomic replacement in Escherichia coli K-12 using covalently closed circular plasmid DNA. Gene. 1990;96:29-36 pubmed..It is reported that such mutants may be constructed without linearizing plasmid DNA, as described previously. ..
- Wood D, Darlison M, Wilde R, Guest J. Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli. Biochem J. 1984;222:519-34 pubmed..iron-sulphur protein gene (sdhB) these genes form an operon (sdhCDAB) situated between the citrate synthase gene (gltA) and the 2-oxoglutarate dehydrogenase complex genes (sucAB): gltA-sdhCDAB-sucAB...
- Davis B, Gilvarg C. The role of the tricarboxylic acid cycle in acetate oxidation in Escherichia coli. J Biol Chem. 1956;222:307-19 pubmed
- Walsh K, Schena M, Flint A, Koshland D. Compensatory regulation in metabolic pathways--responses to increases and decreases in citrate synthase levels. Biochem Soc Symp. 1987;54:183-95 pubmed..The interplay between citrate synthase and isocitrate dehydrogenase illustrates how living systems can compensate for variations in their internal environment. ..
- Park S, McCabe J, Turna J, Gunsalus R. Regulation of the citrate synthase (gltA) gene of Escherichia coli in response to anaerobiosis and carbon supply: role of the arcA gene product. J Bacteriol. 1994;176:5086-92 pubmed..In Escherichia coli this enzyme is encoded by the gltA gene...
- Vandedrinck S, Deschamps G, Sablon E, Vandamme E. Metabolic engineering of Escherichia coli: construction and characterization of a gltA (citrate synthase) knockout mutant. Meded Rijksuniv Gent Fak Landbouwkd Toegep Biol Wet. 2001;66:333-6 pubmed..This paper discusses the construction and characterization of an E. coli gltA- knockout mutant...
- Guest J. Hybrid plasmids containing the citrate synthase gene (gltA) of Escherichia coli K12. J Gen Microbiol. 1981;124:17-23 pubmed..coli hybrid plasmids was screened by conjugation for complementation of the citrate synthase lesion of a gltA mutant. Three ColE1-gltA+ plasmids were identified: pLC26-17 (16.3 kilobase pairs), pLC27-18 (16...
- Bloxham D, Herbert C, Giles I, Ner S. The use of bacteriophage M13 carrying defined fragments of the Escherichia coli gltA gene to determine the location and structure of the citrate synthase promoter region. Mol Gen Genet. 1983;191:499-506 pubmedThe gltA gene from Escherichia coli, which encodes citrate synthase, has been located on a 3.24 Kb HindIII/EcoRl restriction fragment. This region contains one restriction site for BamHl and two for BglII...
- Spencer M, Guest J. Molecular cloning of four tricarboxylic acid cyclic genes of Escherichia coli. J Bacteriol. 1982;151:542-52 pubmed..1 kilobases [kb]) from a ColE1 Escherichia coli DNA hybrid plasmid containing the bacterial citrate synthase gene (gltA) was subcloned in both orientations into phage lambda vectors by in vitro recombination...