Disease relevance of gltA

• However, the half-lives of tlc mRNA and gltA mRNA I in recombinant Escherichia coli strains are 2.9 +/- 0.1 and 1.4 +/- 0.1 min, respectively [1].
• Identification of tlc and gltA mRNAs and determination of in situ RNA half-life in Rickettsia prowazekii [1].
• 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 [2].
• icdB mutations map at 16 min, lead to the specific loss of citrate synthase, and are complemented by a prophage containing a gltA+ gene [3].
• Genome sequencing revealed that the Corynebacterium glutamicum genome contained, besides gltA, two additional citrate synthase homologous genes (prpC) located in two different prpDBC gene clusters, which were designated prpD1B1C1 and prpD2B2C2 [4].

High impact information on gltA

• [13C]propionate oxidation in wild-type and citrate synthase mutant Escherichia coli: evidence for multiple pathways of propionate utilization [5].
• The active-site aspartic acid residue, Asp-362, of Escherichia coli citrate synthase was changed by site-directed mutagenesis to Glu-362, Asn-362 or Gly-362 [6].
• 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 [7].
• It catalyzes the condensation of oxaloacetate and acetyl coenzyme A to produce citrate plus coenzyme A. In Escherichia coli this enzyme is encoded by the gltA gene [8].
• To investigate how gltA expression is regulated, a gltA-lacZ operon fusion was constructed and analyzed following aerobic and anaerobic cell growth on various types of culture media [8].

Chemical compound and disease context of gltA

• Starting with a colicin E1 resistance recombinant plasmid which contains gltA, the gene for citrate synthase in Escherichia coli, we have constructed an ampicillin-resistance plasmid containing the gltA region as a 2.9-kilobase-pair insert in the tetracycline-resistance region of pBR322 [9].
• Acinetobacter anitratum citrate synthase shows hyperbolic saturation with acetyl-CoA (n = 1.8) [10].
• Unlike E. coli citrate synthase, the A. anitratum enzyme does not react with the sulfhydryl reagent 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) in the absence of denaturation [10].
• Acinetobacter anitratum citrate synthase is much more resistant to urea denaturation than the E. coli enzyme is; the resistance of both enzymes to urea is greatly improved in the presence of 1 M KCl [10].

Biological context of gltA

• Nevertheless, B. lactofermentum-modified replicative plasmid DNA can be transformed by electroporation into C. melassecola; thus pCGL519-2, a shuttle plasmid that carries the C. melassecola analogue of E. coli gltA (encoding citrate synthase), was extracted from the former host and electroporated into the latter [11].
• The molecular analysis of the resulting transformants suggests that they result from the integration of a single circular integron molecule by homologous recombination between the gltA regions of the host genome and the integron [11].
• These findings indicate that the regulation of gltA gene expression is complex in meeting the differential needs of the cell for biosynthesis and energy generation under various cell culture conditions [8].
• Knocking out ppc or gltA decreased the maximum cell density by 14% and increased the acetate excretion by 7%, respectively decreased it by 10% [12].
• The nucleotide sequence of this fragment is presented; the inferred amino acid sequence was 70 and 76% identical, respectively, with the citrate synthase sequences from E. coli and Acinetobacter anitratum, two other gram-negative bacteria [13].

Associations of gltA with chemical compounds

• In contrast, CS could not use propionyl-CoA as a substrate [2].
• Conversion of citrate synthase into citryl-CoA lyase as a result of mutation of the active-site aspartic acid residue to glutamic acid [6].
• 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) [14].

Analytical, diagnostic and therapeutic context of gltA

• Sequence analysis indicates that gltA encodes a 481- amino acid protein (53,269 Da) [15].

References