Disease relevance of tartaric acid

• Malate dehydrogenase from Pseudomonas putida was A-specific, and the proposition is discussed that the common A-stereospecificity among the dehydrogenases involved in meso-tartrate metabolism reflects their origin from malate dehydrogenase [1].
• Physiological basis for meso-tartrate sensitivity in some strains of Salmonella typhimurium [2].

High impact information on tartaric acid

• As a comparison, native fumarase was crystallized in the presence of the competitive inhibitor, meso-tartrate [3].
• These data are consistent with a model in which the course of the reaction with (+)-tartrate and meso-tartrate is dictated by the coordination of the substrate hydroxyls to the active site Mn2+ [4].
• D-Glycerate and CO2 are formed from meso-tartrate in a reaction that is formally a decarboxylation with no net oxidation or reduction [5].
• C-R intermediates of the tricarboxylic acid cycle or compounds readily converted to them and substrates metabolized independently of the C-6 part of the cycle spared bacteria from the inhibitory effects of meso-tartrate when added to cultures along with meso-tartrate [2].
• Various phenotypic features, such as denitrification, growth at 4 degrees C or 41 degrees C, trigonelline assimilation, alpha-L-glutamyl-L-histidine arylarmidase activity, growth on benzoate and meso-tartrate were found to differentiate Pseudomonas jessenii from Pseudomonas mandelii and from other Pseudomonas species [6].

Associations of tartaric acid with other chemical compounds

• To explain these unidirectional effects it is suggested that the control site of "malic' enzyme binds organic acids (including meso-tartrate) which activate the enzyme. meso-Tartrate, however, competes with malate for the active site and thus inhibits the oxidative decarboxylation of malate [7].

References