Biodegradative ornithine decarboxylase of Escherichia coli. Purification, properties, and pyridoxal 5'-phosphate binding site

Applebaum, Deborah M.; Sabo, Donna L.; Fischer, Edmond H.; Morris, David R.

doi:10.1021/bi00687a025

Cited by 74 publications

(38 citation statements)

References 32 publications

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“…Second, if internal pH were considerably higher than our measurements indicated, then other amino acid decarboxylases with higher pH optima, such as ornithine decarboxylase (pH optimum 7.0), might be expected to function as effective acid resistance systems. However, ornithine decarboxylase does not protect cells at pH 2.5, a finding we attribute to the high pH optimum limiting enzymatic function at the acidic internal pH reported here (3,22). The situation with lysine decarboxylase (CadA) further supports the hypothesis.…”

Section: Discussionsupporting

confidence: 70%

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Escherichia coli Glutamate- and Arginine-Dependent Acid Resistance Systems Increase Internal pH and Reverse Transmembrane Potential

2004

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Due to the acidic nature of the stomach, enteric organisms must withstand extreme acid stress for colonization and pathogenesis. Escherichia coli contains several acid resistance systems that protect cells to pH 2. One acid resistance system, acid resistance system 2 (AR2), requires extracellular glutamate, while another (AR3) requires extracellular arginine. Little is known about how these systems protect cells from acid stress. AR2 and AR3 are thought to consume intracellular protons through amino acid decarboxylation. Antiport mechanisms then exchange decarboxylation products for new amino acid substrates. This form of proton consumption could maintain an internal pH (pH i ) conducive to cell survival. The model was tested by estimating the pH i and transmembrane potential (⌬⌿) of cells acid stressed at pH 2.5. During acid challenge, glutamate-and arginine-dependent systems elevated pH i from 3.6 to 4.2 and 4.7, respectively. However, when pH i was manipulated to 4.0 in the presence or absence of glutamate, only cultures challenged in the presence of glutamate survived, indicating that a physiological parameter aside from pH i was also important. Measurements of ⌬⌿ indicated that amino acid-dependent acid resistance systems help convert membrane potential from an inside negative to inside positive charge, an established acidophile strategy used to survive extreme acidic environments. Thus, reversing ⌬⌿ may be a more important acid resistance strategy than maintaining a specific pH i value.

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Section: Discussionsupporting

confidence: 70%

“…Carbonic anhydrase essentially adds water, not free protons, to CO 2 to make carbonic acid (H 2 CO 3 ); carbonic acid can then dissociate to HCO 3 Ϫ and H ϩ . Because the pK a of this reaction is 6.5, an internal pH that is estimated to be between 4.2 and 4.7 will prevent this dissociation (18).…”

Section: Discussionmentioning

confidence: 99%

Escherichia coli Glutamate- and Arginine-Dependent Acid Resistance Systems Increase Internal pH and Reverse Transmembrane Potential

2004

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“…Degradative basic amino acid decarboxylation systems are quite common among Gram-negative Enterobacteriaceae, where they play a role in acid stress resistance (34,35,36). Different systems consisting of a decarboxylase and a precursor/product exchanger have been found for lysine/cadaverine (LDC) (cadAB), arginine/ agmatine (adiAC), and ornithine/putrescine (ODC) (speF/potE).…”

Section: Discussionmentioning

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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“…For assay of inducible ornithine decarboxylase, cell extracts were obtained from 100 ml cultures grown in the medium described by Applebaum et al (1975). Bacteria were collected, washed and then resuspended in 1 ml of 0.05 M-Mes buffer, pH 6.3, containing 1 mM-dithiothreitol and 2.4 mM-EDTA.…”

Section: Experimental Materialsmentioning

confidence: 99%

“…Several studies on the decarboxylation of ornithine and arginine have indicated that each of these reactions can be catalysed by two different enzymes: one is a constitutive 'biosynthetic' decarboxylase present in cells grown in neutral minimal medium, and the other is a 'biodegradative' enzyme induced in certain strains cultivated in acid media containing high concentrations ofthe respective undecarboxylated substrate, ornithine or arginine (Gale, 1946;Morris & Fillingame, 1974;Applebaum et al, 1975Applebaum et al, , 1977.…”

Section: Introductionmentioning

confidence: 99%

A probable new pathway for the biosynthesis of putrescine in Escherichia coli

Cataldi¹,

Algranati²

1986

Biochemical Journal

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Some cultures of Escherichia coli BGA8, a mutant unable to synthesize putrescine, showed a change of behaviour and could grow almost equally well in either the absence or the presence of polyamines after repeated periods of polyamine starvation. Experiments in vivo with radioactive precursors showed that the bacteria which evaded the polyamine requirement had recovered their ability to synthesize putrescine from glucose or glutamic acid, but not from ornithine or arginine. These results are in agreement with the fact that the polyamine-independent cells were still deficient in the enzymes ornithine decarboxylase and agmatinase. Our findings seem to indicate the existence of a new pathway to synthesize putrescine which does not involve ornithine or arginine as intermediates.

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Biodegradative ornithine decarboxylase of Escherichia coli. Purification, properties, and pyridoxal 5'-phosphate binding site

Cited by 74 publications

References 32 publications

Escherichia coli Glutamate- and Arginine-Dependent Acid Resistance Systems Increase Internal pH and Reverse Transmembrane Potential

Escherichia coli Glutamate- and Arginine-Dependent Acid Resistance Systems Increase Internal pH and Reverse Transmembrane Potential

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

A probable new pathway for the biosynthesis of putrescine in Escherichia coli

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