Pyruvic acid bacterial production

FIGURE 3.3. Illustration of some major pathways and end products of the bacterial fermentation of sugars from pyruvic acid (Stanier et al., 1986). 

The literature concerning malo—lactic fermentation—bacterial conversion of L-malic acid to L-lactic acid and carbon dioxide in wine—is reviewed, and the current concept of its mechanism is presented. The previously accepted mechanism of this reaction was proposed from work performed a number of years ago subsequently, several workers have presented data which tend to discount it. Currently, it is believed that during malo-lactic fermentation, the major portion of malic acid is directly decarboxylated to lactic acid while a small amount of pyruvic acid (and reduced coenzyme) is formed as an end product, rather than as an intermediate. It is suspected that this small amount of pyruvic acid has extremely important consequences on the intermediary metabolism of the bacteria. 

Certain bacterial strains convert propylene glycol to pyruvic acid in the presence of thiamine (15) other strains do the conversion without thiamine (16). Propylene oxide is the principal product of the reaction of propylene glycol over a cesium impregnated silica gel at 360°C in the presence of methyl ethyl ketone and xylene (17). 

Lund H (1957) Electroorganic preparations. IV. Oxidation of aromatic hydrocarbons. Acta Chim Scand 11 1323-1130 Lwoff A, Ionesco H (1947) Replacement of potassium by rubidium and cesium in the bacterial production of pyruvic acid from malic acid. Comptes Rendues Academic Sciences 225 77-79... 

The metabolic pathway for bacterial sugar fermentation proceeds through the Embden-Meyerhof-Paranas (EMP) pathway. The pathway involves many catalysed enzyme reactions which start with glucose, a six-carbon carbohydrate, and end with two moles of three carbon intermediates, pyruvate. The end pyruvate may go to lactate or be converted to acetyl CoA for the tricarboxylic acid (TCA) cycle. The fermentation pathways from pyruvate and the resulting end products are shown in Figures 9.7 and 9.8. 

A similar stereochemical question as in the /8-replacement reactions can be asked in the a, /8-eliminations where the group X is replaced by a hydrogen, i.e., is the proton added at C-/8 of the PLP-aminoacrylate on the same face from which X departed or on the opposite face This question has been answered for a number of enzymes which generate either a-ketobutyrate or pyruvate as the keto acid product. Crout and coworkers [119,120] determined the steric course of proton addition in the a,/8-elimination of L-threonine by biosynthetic L-threonine dehydratase and of D-threonine by an inducible D-threonine dehydratase, both in Serratia marcescens. Either substrate, deuterated at C-3, was converted in vivo into isoleucine, which was compared by proton NMR to a sample prepared from (3S)-2-amino[3-2H]butyric acid. With both enzymes the hydroxyl group at C-3 was replaced by a proton in a retention mode. Although this has not been established with certainty, it is likely that both enzymes, like other bacterial threonine dehydratases [121], contain PLP as cofactor. Sheep liver L-threonine dehydratase, on the other hand, is not a PLP enzyme but contains an a-ketobutyrate moiety at the active site [122], It replaces the hydroxyl group of L-threonine with H in a retention mode, but that of L-allothreonine in an inversion mode [123]. Snell and coworkers [124] established that the replacement of OH by H in the a, /8-elimination of D-threonine catalyzed by the PLP-containing D-serine dehydratase from E. coli also proceeds in a retention mode. They... 

Lysine is formed in bacteria by decarboxylation of meso-diamino-pimelic acid (Fig. 24-14). Glycine is decarboxylated oxidatively in mitochondria in a sequence requiring lipoic acid and tetrahydrofolate as well as PLP (Fig. 15-20). A methionine decarboxylase has been isolated in pure form from a fem. ° The bacterial dialkylglycine decarboxylase is both a decarboxylase and an aminotransferase which uses pyruvate as its second substrate forming a ketone and L-alanine as products (See Eq. 

Production of organic acids is found among various bacterial and fungal species. This is particularly common among all lactic acid bacteria (LAB) (Vesterlund et al., 2004). Heterofermentative LAB are able to ferment various organic acids, predominantly citrate, malate, and pyruvate (Zaunmuller et al., 2006). In various species and strains of LAB, organic acid production may, however, vary. For example, in Lactococcus ladus pyruvate is partially converted to a-acetolactate when electron acceptors (such as citrate) are present, whereas Lactobacillus sanfranciscensis... 

A variety of monosaccharides (hexoses or pentoses) can be fermented to produce 2,3-BD (Syu, 2001). In bacterial metabolism, monosaccharides must first be converted to pyruvate before generation of major products. From glucose, pyruvate is formed in a relatively simple manner via the Embden-Meyerhof pathway (glycolysis). In contrast, the production of pyruvate from pentoses must proceed via a combination of the pentose phosphate and Embden-Meyerhof pathways (Jansen and Tsao, 1983). In addition to 2,3-BD, the pyruvate produced from the monosaccharides is then channeled into a mixture of acetate, lactate, formate, succinate, acetoin, and ethanol, through the mixed acid-2,3-BD fermentation pathway (Ji et al., 2011a). 

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