Enterococcus faecalis glutathione reductase: purification, characterization and expression under normal and hyperbaric O2 conditions

Patel, Mehul

doi:10.1016/s0378-1097(98)00325-5

Cited by 6 publications

(7 citation statements)

References 26 publications

(16 reference statements)

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“…2). The absence of a specific glutathione reduction system in the Campylobacterales and many genera of Firmicutes (Patel et al 1998) may explain the close evolutionary relationship between the TrxB 1 of these two bacterial groups.…”

Section: Discussionmentioning

confidence: 99%

Identification of disulfide reductases in Campylobacterales: a bioinformatics investigation

Kaakoush

Sterzenbach

Miller

et al. 2007

Antonie van Leeuwenhoek

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Disulfide reductases of host-colonising bacteria are involved in the expression of virulence factors, resistance to drugs, and elimination of toxic compounds. Large-scale genome analyses of 281 prokaryotes identified CXXC and CXXC-derived motifs in each microorganism. The total number of these motifs showed correlations with genome size and oxygen tolerance of the prokaryotes. Specific bioinformatic analyses served to identify putative disulfide reductases in the Campylobacterales Campylobacter jejuni, Helicobacter pylori, Wolinella succinogenes and Arcobacter butzleri which colonise the gastrointestinal tract of higher animals. Three filters applied to the genomes of these species yielded 35, 25, 28 and 34 genes, respectively, encoding proteins with the characteristics of disulfide reductases. Ten proteins were common to the four species, including four belonging to the thioredoxin system. The presence of thioredoxin reductase activities was detected in the four bacterial species by observing dithiobis-2-nitrobenzoic acid reduction with beta-nicotinamide adenine dinucleotide phosphate as cofactor. Phylogenetic analyses of the thioredoxin reductases TrxB(1) and TrxB(2) of the four Campylobacterales were performed. Their TrxB(1) proteins were more closely related to those of Firmicutes than to the corresponding proteins of other Proteobacteria. The Campylobacterales TrxB(2) proteins were closer to glutathione reductases of other organisms than to their respective TrxB(1) proteins. The phylogenetic features of the Campylobacterales thioredoxin reductases suggested a special role for these enzymes in the physiology of these bacteria.

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Section: Discussionmentioning

confidence: 99%

Identification of disulfide reductases in Campylobacterales: a bioinformatics investigation

Kaakoush

Sterzenbach

Miller

et al. 2007

Antonie van Leeuwenhoek

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“…Dismutation of any intracellular superoxide is catalysed by an inducible manganese superoxide dismutase (Britton et al ., 1978). In addition to these reactive oxygen species scavengers, E. faecalis is unusual as a Gram‐positive bacterium in the ability to synthesize glutathione and express glutathione reductase (Patel et al ., 1998; Sherrill and Fahey, 1998). Glutathione is a key reductant for several different classes of enzymes that can reduce hydrogen peroxide or hydroperoxides to form water and corresponding alcohols.…”

Section: Discussionmentioning

confidence: 99%

Extracellular superoxide production by Enterococcus faecalis requires demethylmenaquinone and is attenuated by functional terminal quinol oxidases

Huycke

Moore

Joyce

et al. 2001

Molecular Microbiology

174

115

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SummaryThe intestinal commensal bacterium, Enterococcus faecalis, is unusual among prokaryotic organisms in its ability to produce substantial extracellular superoxide. Transposon mutagenesis, allelic replacement, and electron spin resonance (ESR)-spin trapping showed that superoxide production and generation of derivative hydroxyl radical were dependent on membrane-associated demethylmenaquinone. Extracellular superoxide was generated through univalent reduction of oxygen by reduced demethylmenaquinone. Moreover, extracellular superoxide production was inhibited by exogenous haematin, an essential cofactor for cytochrome bd, and by fumarate, a substrate for fumarate reductase. As integral membrane quinol oxidases, cytochrome bd and fumarate reductase redox cycle demethylmenaquinone, and are necessary for aerobic and anaerobic respiration respectively. A rat model of intestinal colonization demonstrated that conditions exist in the mammalian intestinal tract that permit a mode of respiration for E. faecalis that results in the formation of hydroxyl radical. These results identify and characterize the mechanism by which E. faecalis generates extracellular free radicals.

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“…), E. faecalis (Patel et al . ) and activity has been reported in many lactobacilli species (Girgis et al . ; Jänsch et al .…”

Section: Discussionmentioning

confidence: 87%

Glutathione biosynthesis and activity of dependent enzymes in food-grade lactic acid bacteria harbouring multidomain bifunctional fusion gene (gshF)

et al. 2017

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Enterococcus faecalis glutathione reductase: purification, characterization and expression under normal and hyperbaric O2 conditions

Cited by 6 publications

References 26 publications

Identification of disulfide reductases in Campylobacterales: a bioinformatics investigation

Identification of disulfide reductases in Campylobacterales: a bioinformatics investigation

Extracellular superoxide production by Enterococcus faecalis requires demethylmenaquinone and is attenuated by functional terminal quinol oxidases

Glutathione biosynthesis and activity of dependent enzymes in food-grade lactic acid bacteria harbouring multidomain bifunctional fusion gene (gshF)

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