Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.3.3.1 (citrate synthase)
 4,488 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Citrate synthase activity of Saccharomyces cerevisiae was determined by a radioactive assay procedure and the reaction product, 14C-citric acid, was identified by chromatographic techniques. ATP, d-ATP, GTP and NADH were most inhibitory to the citrate synthase invitro. The activity was inhibited to a lesser extent by ADP, UTP, and NADP whereas, AMP and CTP were much less inhibitory. NADH, like NAD, glutamic acid, glutamine, arginine, ornithine, proline, aspartic acid and alpha-ketoglutarate exhibited no inhibition. These results have been discussed in the light of the role of citrate synthase for the energy metabolism and glutamic acid biosynthesis.
 ...
PMID:Regulation of citrate synthase activity of Saccharomyces cerevisiae. 0

Cultures of isocitrate dehydrogenase-deficient (icd) mutants were overgrown by double mutants (icd glt) lacking citrate synthase activity also. The icd mutants grew more slowly than wild-type cells or the double mutants because they accumulated an inhibitory metabolite (possibly citrate). Intracellular citrate levels were several hundred-fold higher in icd cells than in wild-type or icd glt cells. Final growth yields of the wild type and the icd mutant on limiting glucose were equivalent and greater than the growth yield of icd glt double mutants. The icd gene mapped between 60 and 74 min. icd mutants were resistant to nalidixic acid, but glt and icd glt mutants and wild-type cells were sensitive, indicating that resistance results from accumulation of isocitrate, citrate, or a derivative of these compounds.
 ...
PMID:Selection for citrate synthase deficiency in icd mutants of Escherichia coli. 77 50

Relationship of citrate synthase (EC 4.1.3.7) to the biosynthesis of glutamic acid was investigated by characterizing a new glutamic acid auxotroph FL100-D1 (glu 3) of Saccharomyces cerevisiae. Nutritional requirement of the mutant was satisfied by L-glutamic acid, L-glutamic acid peptide as well as several analogs of glutamic acid, but not by proline, ornithine, arginine, lysine or aspartic acid. The mutant was unable to utilize nonfermentable carbon sources, glycerol, acetate or lactate. Mutant glu3 unlike aconitaseless glutamic acid auxotroph glu 1, failed to accumulate 14C-citric acid in vivo from 1-14C-sodium acetate or U-14C-glutamic acid. Both spectrophotometric and radioactive assay procedures demonstrated a lack of significant citrate synthase activity in the dialysed extract of the mutant compared to the wild type strain. Mutant glu 3 complemented with glu 1 and glu 2 individually in vivo and exhibited a significant aconitase (EC 4.2.1.3) activity in vitro.
 ...
PMID:Citrate synthaseless glutamic acid auxotroph of Saccharomyces cerevisiae. 110 43

A convenient procedure for the synthesis and purification of oligonucleotides is described. 16-base long primers synthesised by this method were used to investigate DNA sequencing using plasmid DNA as a template. This allowed the further analysis of the E. coli glt A sequence coding for citrate synthase and enabled determination of the 5'-non-coding regulatory region of the aminoglycoside phosphotransferase gene.
 ...
PMID:The synthesis and use of oligodeoxynucleotides in plasmid DNA sequencing. 351 4

The synthesis of citric and glutamic acids by extracts of Chloropseudomonas ethylicum was studied with labeled precursors. When acetyl-coenzyme A-1-(14)C was used as substrate, only 0.1% of the total radioactivity was found in the C-5 position of citric acid; whereas, with oxalacetate-4-(14)C as substrate, 100% of the total radioactivity was found in C-5. These results demonstrated that the Chloropseudomonas citrate synthetase had an absolute stereospecificity, identical to that of the pig heart synthetase. The distribution of radioactivity in the glutamic acid synthesized from acetyl-coenzyme A-1-(14)C was 0% in C-1 and 94.0% in C-5; whereas the glutamic acid formed from oxalacetate-4-(14)C contained 89.6% in C-1 and 0.5% in C-5. This distribution is entirely consistent with the biosynthesis of glutamic acid from citric acid via aconitase, d(s)-isocitrate, and l-glutamate dehydrogenases. The presence of l-glutamate dehydrogenase in extracts was demonstrated. The stereospecificity of the citrate synthetase and the pattern of glutamate labeling further establish that the aconitase of Chloropseudomonas is completely stereospecific.
 ...
PMID:Stereospecificity of citrate synthetase in relation to glutamate biosynthesis by extracts of Chloropseudomonas ethylicum. 564 42

Cell-free extracts of Acetobacter suboxydans were prepared which were capable of condensing alpha-ketoisovalerate with (14)C-labeled acetyl-coenzyme A to yield (14)C-labeled alpha-isopropylmalate. The product of the reaction was isolated by paper and column chromatography and was characterized by recrystallization with synthetic alpha-isopropylmalic acid to constant specific radioactivity. The formation of alpha-isopropylmalate by extracts of A. suboxydans plus the ability of the organism to grow in a simple glucose-glycerol medium containing glutamic acid as the only amino acid indicate that the pathway for leucine biosynthesis shown to exist in yeast and Salmonella typhimurium also occurs in A. suboxydans. As a comparison, the condensation of oxalacetate and ((14)C) acetyl-coenzyme A to yield ((14)C) citric acid was shown, by similar means, to occur in A. suboxydans. This is of interest since the existence of this classical condensing enzyme has hitherto not been demonstrated in this organism. This reaction was further demonstrated in cell-free extracts of A. suboxydans by means of a spectrophotometric assay at 232 mmu which measured the cleavage of the carbon-sulfur bond of acetyl-coenzyme A in the presence of oxalacetate. Comparison of the specific activities of crude cell-free extracts indicated a much more extensive occurrence of this reaction in yeast than in A. suboxydans.
 ...
PMID:Biosynthesis of alpha-isopropylmalic and citric acids in Acetobacter suboxydans. 603 58

In work previously reported (J. A. Gutierrez, P. J. Crowley, D. P. Brown, J. D. Hillman, P. Youngman, and A. S. Bleiweis, J. Bacteriol. 178:4166-4175, 1996), a Tn917 transposon-generated mutant of Streptococcus mutans JH1005 unable to synthesize glutamate anaerobically was isolated and the insertion point of the transposon was determined to be in the icd gene encoding isocitrate dehydrogenase (ICDH). The intact icd gene of S. mutans has now been isolated from an S. mutans genomic plasmid library by complementation of an icd mutation in Escherichia coli host strain EB106. Genetic analysis of the complementing plasmid pJG400 revealed an open reading frame (ORF) of 1,182 nucleotides which encoded an enzyme of 393 amino acids with a predicted molecular mass of 43 kDa. The nucleotide sequence contained regions of high (60 to 72%) homology with icd genes from three other bacterial species. Immediately 5' of the icd gene, we discovered an ORF of 1,119 nucleotides in length, designated citZ, encoding a homolog of known citrate synthase genes from other bacteria. This ORF encoded a predicted protein of 372 amino acids with a molecular mass of 43 kDa. Furthermore, plasmid pJG400 was also able to complement a citrate synthase (gltA) mutation of E. coli W620. The enzyme activities of both ICDH, found to be NAD+ dependent, and citrate synthase were measured in cell extracts of wild-type S. mutans and E. coli mutants harboring plasmid pJG400. The region 5' from the citZ gene also revealed a partial ORF encoding 264 carboxy-terminal amino acids of a putative aconitase gene. The genetic and biochemical evidence indicates that S. mutans possesses the enzymes required to convert acetyl coenzyme A and oxalacetate to alpha-ketoglutarate, which is necessary for the synthesis of glutamic acid. Indeed, S. mutans JH1005 was shown to assimilate ammonia as a sole source of nitrogen in minimal medium devoid of organic nitrogen sources.
 ...
PMID:Role of the citrate pathway in glutamate biosynthesis by Streptococcus mutans. 900 16

The effects of acute exercise on myocardial content of glut-1 and glut-4 transporters, insulin and IGF-1 receptors were assessed in control and chronically exercised 24-month-old C57B1/6 mice. Myocardial glut-1, glut-4, insulin receptor (Ins R) and insulin like growth factor-1 receptor (IGF-1 R) protein levels were unaffected by 36 weeks of chronic exercise. However, myocardial protein content of glut-1, but not glut-4, was increased 12 h following an acute exercise bout in control (46%) and chronically exercised (83%) aged animals. This increased glut-1 response following acute exercise occurred despite the finding that the chronic exercise failed to increase cardiac or skeletal muscle oxidative capacity as indicated by no change in citrate synthase activity. Myocardial IGF-1 R content was unaffected by acute exercise whereas Ins R protein content was decreased 12 h following the acute exercise bout in the chronically exercised (-52%) and control (-28%) animals. The effect of acute exercise on the protein content of glut-1 and Ins R was 80 and 84% greater respectively, in the chronically exercised animals. This suggests that the amplitude of the expression of these two proteins may be increased by chronic exercise, thus constituting a form of adaptation.
 ...
PMID:Resistance of the aged myocardium to exercise-induced chronic changes in glucose transport related protein content. 1058 Jun 96

We identified a 14-kb pyruvate carboxylase gene-containing fragment from a lactococcal C2-lambda phage genomic library. Downstream of the pyruvate carboxylase gene-containing fragment, a gene cluster coding for open reading frames displaying extensive homology to citrate synthase, aconitase, and a truncated isocitrate dehydrogenase was identified. However, the truncation was shown to have occurred during the cloning by two noncontiguous Sau3AI fragments ligating together. The lactococcal citrate synthase gene consisted of 1323 bp and encoded a 441-amino acid citrate synthase protein. The lactococcal aconitase gene was 2544 bp and encoded an 848-amino acid protein. Corresponding to the complete citrate synthase gene, citrate synthase activity was detected in Lactococcus lactis ssp. lactis C2. Isocitrate dehydrogenase activity was found to be missing in Lactococcus lactis C2, suggesting that the gene may be incomplete or is not expressed, resulting in a requirement for glutamic acid in lactococci.
 ...
PMID:Identification of a gene cluster encoding Krebs cycle oxidative enzymes linked to the pyruvate carboxylase gene in Lactococcus lactis ssp. lactis C2. 1100 18

A prospective study was performed (June 1999 to May 2001) to determine the incidence of infective endocarditis (IE) due to Bartonella in dogs in northern California and to compare these patients with other dogs with IE. IE was diagnosed antemortem based on clinical signs and echocardiography in 18 dogs. The etiologic agent was Bartonella sp. in 5 dogs (28%) and was diagnosed by high seroreactivity to Bartonella (titer > 1:512; range, 1:1,024-1:4,096); and confirmed postmortem by positive polymerase chain reaction (PCR)-restriction fragment length polymorphism (RFLP) from the infected valve and partial DNA sequencing of the citrate synthase gene (glt A). Conventional bacteria were causative agents in 7 dogs (39%). An etiologic agent was not identified in 6 dogs (33%). Bartonella vinsonii berkhoffii (n = 3), B clarridgeiae (n = 1), and a B clarridgeiae-like organism (n = 1) were identified. Blood culture was positive only for the IE case due to B clarridgeiae. All dogs with IE due to Bartonella were also seroreactive to Anaplasma phagocytophilum. All dogs with IE due to Bartonella had lesions only on the aortic valve. Of the cases of IE not due to Bartonella, 31% involved the aortic valve, 61% the mitral valve, and 8% both valves. Dogs with mitral valve IE lived longer than all dogs with aortic valve IE (P = .004) and dogs with IE of the aortic valve due to Bartonella (P = .002). In conclusion, Bartonella is a common cause of IE in dogs of northern California. A high Bartonella serologic titer (> 1:512) is useful antemortem to diagnose aortic valve IE due to Bartonella.
 ...
PMID:A prospective study of canine infective endocarditis in northern California (1999-2001): emergence of Bartonella as a prevalent etiologic agent. 1476 33


1 2 Next >>