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Gene Review:

gltA - type II citrate synthase

Escherichia coli O157:H7 str. EDL933

Ewering, C. et al., Noda, S. et al., Santoro, N. et al., Connaris, H. et al., Francois, J.A. et al., et al.

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Disease relevance of gltA

2-Methylcitrate synthase (2-MCS1) and citrate synthase (CS) of Ralstonia eutropha strain H16 were separated by affinity chromatography and analyzed for their substrate specificities [1].
High-level expression was achieved in Escherichia coli and the recombinant citrate synthase was purified to homogeneity using a heat step and dye-ligand affinity chromatography [2].

High impact information on gltA

A. aceti citrate synthase (AaCS), a hexameric type II citrate synthase, is required for acetic acid resistance and, therefore, would be expected to function at low pH [3].
Genetic and biochemical analyses of the mutant revealed the downregulation of many TCA cycle enzymes, including citrate synthase, and the upregulation of the pyruvate dehydrogenase complex in both transcription and enzyme activities [4].
The production of acetyl-CoA was coupled to citrate synthase, which produced citrate and coenzyme A. The amount of coenzyme A formed was detected using 5,5'-dithiobis(2-nitrobenzoic acid) (Ellman's reagent) [5].
In contrast, CS could not use propionyl-CoA as a substrate [1].
Knocking out ppc or gltA decreased the maximum cell density by 14% and increased the acetate excretion by 7%, respectively decreased it by 10% [6].

References

Occurrence and expression of tricarboxylate synthases in Ralstonia eutropha. Ewering, C., Brämer, C.O., Bruland, N., Bethke, A., Steinbüchel, A. Appl. Microbiol. Biotechnol. (2006) [Pubmed]
Cloning and overexpression in Escherichia coli of the gene encoding citrate synthase from the hyperthermophilic Archaeon Sulfolobus solfataricus. Connaris, H., West, S.M., Hough, D.W., Danson, M.J. Extremophiles (1998) [Pubmed]
Structure of a NADH-Insensitive Hexameric Citrate Synthase that Resists Acid Inactivation. Francois, J.A., Starks, C.M., Sivanuntakorn, S., Jiang, H., Ransome, A.E., Nam, J.W., Constantine, C.Z., Kappock, T.J. Biochemistry (2006) [Pubmed]
Alterations of Cellular Physiology in Escherichia coli in Response to Oxidative Phosphorylation Impaired by Defective F1-ATPase. Noda, S., Takezawa, Y., Mizutani, T., Asakura, T., Nishiumi, E., Onoe, K., Wada, M., Tomita, F., Matsushita, K., Yokota, A. J. Bacteriol. (2006) [Pubmed]
A high-throughput screening assay for the carboxyltransferase subunit of acetyl-CoA carboxylase. Santoro, N., Brtva, T., Roest, S.V., Siegel, K., Waldrop, G.L. Anal. Biochem. (2006) [Pubmed]
Metabolic characterisation of E. coli citrate synthase and phosphoenolpyruvate carboxylase mutants in aerobic cultures. De Maeseneire, S.L., De Mey, M., Vandedrinck, S., Vandamme, E.J. Biotechnol. Lett. (2006) [Pubmed]

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