The Occurrence and Distribution of Amino-acid Decarboxylases within the Genus Lactobacillus

Rodwell, A. W.

doi:10.1099/00221287-8-2-224

Cited by 73 publications

(33 citation statements)

References 8 publications

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“…In the case of histidine decarboxylation by L. buchnen ST2A, this is accomplished by an electrogenic antiport mechanism, whereby amino acid and amine are transported by one Z+1 carrier in the exchange mode. It is likely that other amino (R-H) acid decarboxylation reactions described in the literature (6,9,12,20,21,24), in which the amine is excreted in large quantities, are involved in generation of metabolic energy or maintenance of pH by using such a transport mechanism as > COO just described. FIG.…”

Section: Discussionmentioning

confidence: 99%

Generation of a proton motive force by histidine decarboxylation and electrogenic histidine/histamine antiport in Lactobacillus buchneri

et al. 1993

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Lactobaciflus buchneri ST2A vigorously decarboxylates histidine to the biogenic amine histamine, which is excreted into the medium. Cells grown in the presence of histidine generate both a transmembrane pH gradient, inside alkaline, and an electrical potential (A*), inside negative, upon addition of histidine. Studies of the mechanism of histidine uptake and histamine excretion in membrane vesicles and proteoliposomes devoid of cytosolic histidine decarboxylase activity demonstrate that histidine uptake, histamine efflux, and histidine/ histamine exchange are electrogenic processes. Histidine/histamine exchange is much faster than the unidirectional fluxes of these substrates, is inhibited by an inside-negative A* and is stimulated by an inside positive A*. These data suggest that the generation of metabolic energy from histidine decarboxylation results from an electrogenic histidine/histamine exchange and indirect proton extrusion due to the combined action of the decarboxylase and carrier-mediated exchange. The abundance of amino acid decarboxylation reactions among bacteria suggests that this mechanism of metabolic energy generation and/or pH regulation is widespread.Several precursor/product antiport mechanisms have been shown or were anticipated to be involved in generation of metabolic energy (16). Metabolic energy can be obtained from these mechanisms by substrate level phosphorylation (5,17) or by the formation of transmembrane ion gradients (ion and proton motive force). Characteristic for all of these precursor/product antiport mechanisms is that the product is structurally similar to the precursor. Transport of precursor and product can be catalyzed by one membrane transport protein which binds both precursor and product with high affinity. The usual mode in which these carrier proteins function is that of exchange: i.e., reorientation of the substrate binding site to either side of the membrane takes place while a substrate is bound. When the product is more positively charged than the precursor, this antiport generates an inside-negative electrical potential gradient across the membrane. Two examples of such carriers which have been studied in detail are the oxalate/formate antiporter of Oxalobacter formigenes (22) and the malate/lactate carrier of Lactococcus lactis (18). Because the metabolic conversion from oxalate to formate or from malate to lactate is a decarboxylation whereby the carboxylic group leaves the cytoplasm as neutral carbon dioxide or dihydrogen carbonate, the net effect of metabolism and electrogenic precursor/ product antiport is the extrusion of one proton. Consequently, a proton motive force is generated from the free energy of decarboxylation.A different mechanism by which metabolic energy is generated from a decarboxylation reaction is found in the Na'-translocating oxaloacetate decarboxylase (3). In this system, decarboxylation is catalyzed by a membrane-bound protein which uses the free energy directly to translocate sodium ions across the membrane. In this study, it will b...

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Section: Discussionmentioning

confidence: 99%

Generation of a proton motive force by histidine decarboxylation and electrogenic histidine/histamine antiport in Lactobacillus buchneri

et al. 1993

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“…A complex amino acid decarboxylation metabolism appeared to be one of its most distinctive traits (24). In fact, L. saerimneri 30a is known to be capable of decarboxylating histidine, ornithine, and lysine into the corresponding amines (25).…”

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confidence: 99%

“…To date, no information is available about the genes and proteins responsible for lysine decarboxylation by L. saerimneri 30a. The ability of L. saerimneri 30a to synthesize up to several grams of cadaverine per liter (24,25) makes this strain a good model candidate for the characterization of LDC systems of LAB.…”

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confidence: 99%

Three-Component Lysine/Ornithine Decarboxylation System in Lactobacillus saerimneri 30a

Romano¹,

Trip²,

Lolkema³

et al. 2013

Journal of Bacteriology

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cLactic acid bacteria play a pivotal role in many food fermentations and sometimes represent a health threat due to the ability of some strains to produce biogenic amines that accumulate in foods and cause trouble following ingestion. These strains carry specific enzymatic systems catalyzing the uptake of amino acid precursors (e.g., ornithine and lysine), the decarboxylation inside the cell, and the release of the resulting biogenic amines (e.g., putrescine and cadaverine). This study aimed to identify the system involved in production of cadaverine from lysine, which has not been described to date for lactic acid bacteria. Strain Lactobacillus saerimneri 30a (formerly called Lactobacillus sp. 30a) produces both putrescine and cadaverine. The sequencing of its genome showed that the previously described ornithine decarboxylase gene was not associated with the gene encoding an ornithine/putrescine exchanger as in other bacteria. A new hypothetical decarboxylation system was detected in the proximity of the ornithine decarboxylase gene. It consisted of two genes encoding a putative decarboxylase sharing sequence similarities with ornithine decarboxylases and a putative amino acid transporter resembling the ornithine/putrescine exchangers. The two decarboxylases were produced in Escherichia coli, purified, and characterized in vitro, whereas the transporter was heterologously expressed in Lactococcus lactis and functionally characterized in vivo. The overall data led to the conclusion that the two decarboxylases and the transporter form a three-component decarboxylation system, with the new decarboxylase being a specific lysine decarboxylase and the transporter catalyzing both lysine/cadaverine and ornithine/putrescine exchange. To our knowledge, this is an unprecedented observation of a bacterial three-component decarboxylation system. L actic acid bacteria (LAB) are considered to be the most important human-related bacterial group, due to their ability to colonize mucosal tissues and their involvement in a wide variety of fermented foods. Amino acid decarboxylation systems represent one of the keys to LAB adaptability. Decarboxylation systems consist of a decarboxylase and a precursor/product transmembrane exchanger (1, 2). Their combined action results in amino acid intake, decarboxylation, and release of the corresponding biogenic amine. The pathway results in alkalinization of the cytosol and generation of a proton motive force, which can be exploited for acid stress resistance and/or the production of metabolic energy in the form of ATP. Decarboxylase and transporter genes are generally organized in clusters located on the bacterial chromosome or on plasmids. A decarboxylase with a given amino acid specificity is adjacent to an exchanger with an equally strict amino acid/biogenic amine specificity, as was observed for histidine/histamine (3), tyrosine/tyramine (4), aspartate/alanine (5), ornithine/putrescine (6), and glutamate/␥-aminobutyrate (7) decarboxylation systems.Among biogenic amines, histamine, tyra...

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“…It therefore seems that the ability to produce histamine and tyramine occurs infrequently amongst the bacteria that could be used for malolactic fermentation. Previous investigators have also indicated that only certain specific strains of malo-lactic bacteria possess the ability to decarboxylate histidine and tyrosine (Lagerborg & Clapper, 1952;Rodwell, 1953). Of various malo-lactic bacteria isolated from wine by LafonLafourcade (1975), only one strain of Leuconostoc had the ability to produce histamine.…”

Section: Resultsmentioning

confidence: 99%

Histamine and Tyramine Content of South African Wine

Cilliers¹,

Wyk

2017

SAJEV

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The histamine content of 184 wines and tyramine content of 156 wines, produced in South Africa was measured. The histamine and tyramine content of the wine was found to be similar to those of wines produced in other countries. The average histamine content of South African red wines that had undergone malo-lactic fermentation was more than double that of red wines that had not undergone malo-lactic fermentation. All the red wines containing relatively large amounts of histamine had pH's above 3, 7. Six selected strains of malo-lactic bacteria were tested for their ability to form histamine and tyramine in white and red wine. No histamine or tyramine was formed.

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The Occurrence and Distribution of Amino-acid Decarboxylases within the Genus Lactobacillus

Cited by 73 publications

References 8 publications

Generation of a proton motive force by histidine decarboxylation and electrogenic histidine/histamine antiport in Lactobacillus buchneri

Generation of a proton motive force by histidine decarboxylation and electrogenic histidine/histamine antiport in Lactobacillus buchneri

Three-Component Lysine/Ornithine Decarboxylation System in Lactobacillus saerimneri 30a

Histamine and Tyramine Content of South African Wine

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