Pyruvate bacterial metabolism

Stolz A, H-J Knackmuss (1993) Bacterial metabolism of 5-aminosalicylic acid enzymatic conversion to malate, pyruvate and ammonia. J Gen Microbiol 139 1019-1025. 

Practical and fundamental aspects of malo-lactic fermentation are given. Conditions which winemakers can use for better control of the fermentation, including detailed procedures for inoculation with Leuconostoc oenos ML 34 and for inhibition with fumaric acid, are presented. New information on the role of malic acid decarboxylation in bacterial metabolism and on the enzymatics of malic acid decarboxylation are reviewed. The malic acid decarboxylation seems to involve two pathways a direct decarboxylation of malic to lactic acid with NAD as a coenzyme and a concurrent but small oxidative decarboxylation to pyruvic acid and NADH. How these pathways can bring about the marked stimulation of bacterial growth rate by the malo-lactic reaction and their negligible effect on growth yield are discussed. 

Most known thiamin diphosphate-dependent reactions (Table 14-2) can be derived from the five halfreactions, a through e, shown in Fig. 14-3. Each halfreaction is an a cleavage which leads to a thiamin- bound enamine (center, Fig. 14-3) The decarboxylation of an a-oxo acid to an aldehyde is represented by step b followed by a in reverse. The most studied enzyme catalyzing a reaction of this type is yeast pyruvate decarboxylase, an enzyme essential to alcoholic fermentation (Fig. 10-3). There are two 250-kDa isoenzyme forms, one an a4 tetramer and one with an ( P)2 quaternary structure. The isolation of ohydroxyethylthiamin diphosphate from reaction mixtures of this enzyme with pyruvate52 provided important verification of the mechanisms of Eqs. 14-14,14-15. Other decarboxylases produce aldehydes in specialized metabolic pathways indolepyruvate decarboxylase126 in the biosynthesis of the plant hormone indoIe-3-acetate and ben-zoylformate decarboxylase in the mandelate pathway of bacterial metabolism (Chapter 25).1243/127... 

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). 

After the loss of a H from the o-C atom, stabilization can also be attained by eliminating X" from the -C atom and forming a double bond. In nonenzymic model experiments serine and cysteine react according to this scheme of a, -elimination to produce aminoacrylic acid and eventually pyruvic acid and NH3. And in bacterial metabolism, tryptophan is degraded in this fashion to indole + pyruvic acid -t- NHj. 

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. 

Covalent interconversion of enzymes is well established as a fundamental theme in metabolic regulation. The prototypic reversible interconverting systems include the sequence of phosphorylation/dephosphorylation steps in the activation of mammalian glycogen phosphorylase and pyruvate dehydrogenase as well as the nucleotidyla-tion/denucleotidylation using UTP and ATP in the bacterial glutamine synthetase cascade (see Fig. 1.). 

The principal pathways for the biogenesis and metabolism of histamine are well known. Histamine is formed by decarboxylation of the amino acid, L-histidine, a reaction catalyzed by the enzyme, histidine decarboxylase. This decarboxylase is found in both mammalian and non-mammalian species. The mammalian enzyme requires pyridoxal phosphate as a cofactor. The bacterial enzyme has a different pH optimum and utilizes pyruvate as a cofactor (26.27). 

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. 

There are multienzyme complexes that efficiently catalyze sequential reactions in some metabolic pathways. The overall rate of a sequential reaction is greatly enhanced by the assembly of subunits possessing sequential metabolic activities, because the metabolites are transferred directly from one active site to another without diffusing in the solution.9 Typical examples are the mammalian pyruvate dehydrogenase complex (three catalytic subunits)10 and the bacterial trytophan synthase (two catalytic subunits).11 ... 

TCA cycle. (tricarboxylic acid cycle Krebs cycle citric acid cycle). A series of enzymatic reactions occurring in living cells of aerobic organisms, the net result of which is the conversion of pyruvic acid, formed by anaerobic metabolism of carbohydrates, into carbon dioxide and water. The metabolic intermediates are degraded by a combination of decarboxylation and dehydrogenation. It is the major terminal pathway of oxidation in animal, bacterial, and plant cells. Recent research indicates that the TCA cycle may have predated life on earth and may have provided the pathway for formation of amino acids. 

Sedewitz, B., Schleieer, K. H., Gotz, F. (1984a), Physiological role of pyruvate oxidase in the aerobic metabolism of Lactobacillus plantarum, J. Bacterial. 160, 462-465. 

Pyruvoyl cofactor is derived from the posttranslational modification of an internal amino acid residue, and it does not equilibrate with exogenous pyruvate. Enzymes that possess this cofactor play an important role in the metabolism of biologically important amines from bacterial and eukaryotic sources. These enzymes include aspartate decarboxylase, arginine decarboxylase," phosphatidylserine decarboxylase, . S-adenosylmethionine decarboxylase, histidine decarboxylase, glycine reductase, and proline reductase. ... 

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