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Gene Review:

gltA - type II citrate synthase

Escherichia coli CFT073

Ewering, C. et al., Noda, S. et al., Santoro, N. et al., Wood, D.O. et al., De Maeseneire, S.L. 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].
Recombinant DNA techniques were used to isolate the Rickettsia prowazekii citrate synthase gene on the plasmid vector pBR322 by functional complementation of a gltA mutation of Escherichia coli K-12 [2].
Deletions extending clockwise from kdp as far as the gltA locus were isolated from strains with bacteriophage lambda integrated into kdpD [3].

High impact information on gltA

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]
Expression of the Rickettsia prowazekii citrate synthase gene in Escherichia coli. Wood, D.O., Atkinson, W.H., Sikorski, R.S., Winkler, H.H. J. Bacteriol. (1983) [Pubmed]
Functional organization of the kdp genes of Escherichia coli K-12. Rhoads, D.B., Laimins, L., Epstein, W. J. Bacteriol. (1978) [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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