Disease relevance of 850848-65-6

• The Tricarballylate utilization (tcuRABC) genes of Salmonella enterica serovar Typhimurium LT2 [1].
• The slow rate of tricarballylate metabolism by mixed rumen bacteria and its potential as a magnesium chelator suggest that tricarballylate formation could be an important factor in the hypomagnesemia that leads to grass tetany [2].
• Tricarballylate toxicity has been attributed to its ability to chelate magnesium and to inhibit aconitase, a Krebs cycle enzyme [3].
• trans-Aconitic acid has been implicated in magnesium deficiency of ruminants since the 1960s, but recent experiments indicated that much of it can be converted by rumen bacteria to tricarballylic acid (TCBA) [4].
• E. coli K-12 carrying a plasmid with wild-type alleles of tcuABC grew on tricarballylate, suggesting that the functions of the TcuABC proteins were the only ones unique to S. enterica needed to catabolize tricarballylate [1].

High impact information on 850848-65-6

• Tricarballylate is the causative agent of grass tetany, a ruminant disease characterized by acute magnesium deficiency [3].
• The FAD-dependent tricarballylate dehydrogenase (TcuA) enzyme of Salmonella enterica converts tricarballylate into cis-aconitate [3].
• The tcuC gene is proposed to encode an integral membrane protein whose role is to transport tricarballylate across the cell membrane. tcuC function was sufficient to allow E. coli K-12 to grow on citrate (a tricarballylate analog) but not to allow growth of this bacterium on tricarballylate [1].
• The genes of Salmonella enterica serovar Typhimurium LT2 encoding functions needed for the utilization of tricarballylate as a carbon and energy source were identified and their locations in the chromosome were established [1].
• Ability of Acidaminococcus fermentans to oxidize trans-aconitate and decrease the accumulation of tricarballylate, a toxic end product of ruminal fermentation [5].

Biological context of 850848-65-6

• Analysis of bile showed an absence of hydrolysis products, indicating that hydrolysis occurred only in the gut, resulting in the removal of the tricarballylic acid moiety at the C14-position [6].
• The aim of the present study was to investigate intestinal absorption of tricarballylate using brush-border membrane vesicles (BBMVs) isolated from the proximal jejunum of steers by a Ca2+ precipitation method with subsequent differential centrifugation [7].

Anatomical context of 850848-65-6

• Transport of tricarballylate by intestinal brush-border membrane vesicles from steers [7].
• Oxidation of [14C]acetate by isolated rat liver cells was inhibited to a greater extent by tricarballylate [8].
• Turkey peripheral blood lymphocytes were exposed in vitro for 72 hours to fumonisin B1 (FB1), fumonisin B2 (FB2), hydrolyzed fumonisin B1 (HFB1), moniliformin and tricarballylic acid (TCA) (0.01-25 microg/ml) [9].

Associations of 850848-65-6 with other chemical compounds

• High-pressure liquid chromatography of fermentation products from trans-aconitate incubations revealed a compound that was subsequently identified as tricarballylate [2].
• Neither tricarballylic acid nor hydrolyzed fumonisin B1 inhibited recombinant human argininosuccinate synthetase [10].
• The new fumonisin differs from FB1 in that the tricarballylic acid functionality at the C-15 position of the eicosane backbone is replaced by a ketone and the amino group is acetylated [11].
• Biodegradable elastomeric network polyesters were prepared from multifunctional aliphatic carboxylic acids such as tricarballylic acid (Yt) or meso-1,2,3,4-butanetetracarboxylic acid (Xb) and poly(epsilon-caprolactone) (PCL) diols with molecular weights of 530, 1,250 and 2,000 g.mol-1 [12].

Gene context of 850848-65-6

• (4) A reduction in mobility of the tempo-stearate spin label suggests that the tricarballylic acid (TCA) moieties of FB1 might mimic the structure of polar headgroups in phospholipids [13].
• 4. Tricarballylate was a competitive inhibitor of the enzyme, aconitate hydratase (aconitase; EC 4.2.1.3), and the inhibitor constant, KI, was 0.52 mM [8].
• Insertion of 2-carboxysuccinate and tricarballylic acid fragments into cyclic-pseudopeptides: new antagonists for the human tachykinin NK-2 receptor [14].

Analytical, diagnostic and therapeutic context of 850848-65-6

• The circular dichroism (CD) exciton chirality method was employed for the stereochemical assignment of the tricarballylic acid (TCA) side chains of fumonisin B(1) 1a (FB(1)) [15].

References