Dihydroxy-acid Dehydratase, a (4Fe-4S) Cluster-Containing Enzyme in Escherichia coli: Effects of Intracellular Superoxide Dismutase on Its Inactivation by Oxidant Stress

Brown, Olen R.; Smyk-Randall, Elzbieta M.; Draczynska-Lusiak, B; Fee, James A.

doi:10.1006/abbi.1995.1262

Cited by 37 publications

(18 citation statements)

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“…Brown and Yein (1978) have shown that inhibition of Escherichia coli growth by hyperbaric oxygen results from loss of the ability to synthesize branched-chain amino acids. This seems to be due to the irreversible inactivation of the iron-sulfur protein dihydroxyacid dehydratase, the third common enzyme of branchedchain amino acid biosynthesis (Flint et al 1993;Brown et al 1995). Although destruction of the enzyme is inversely correlated with intracellular levels of superoxide dismutase (Brown et al 1995), the possible participation of the first common enzyme in branched-chain amino acid biosynthesis, ALS, in inactivation of dihydroxyacid dehydratase or growth inhibition remains.…”

Section: Acetolactate Synthase (Bacteria and Plants)mentioning

confidence: 96%

Oxygen toxicity from plants to people

Schloss

2002

Planta

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Over the past 30 years, acute oxygen toxicity in plants, mammals and enteric bacteria has been defined in terms of specific interactions of oxygen with a limited number of molecular targets. At least in the case of plants and mammals, response at the level of the whole organism is a consequence of oxygen's interaction with enzymes that should not exhibit oxygen sensitivity, ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) and glutamate decarboxylase (GAD). In enteric bacteria, inhibition of acetolactate synthase (ALS), or the production of peracetic acid by this enzyme, may be a contributing factor in the inactivation of dihydroxyacid dehydratase and loss of the ability to synthesize branched-chain amino acids under conditions of hyperbaric oxygen. The facile interaction of these enzymes with oxygen has questioned our fundamental understanding of their reaction mechanisms. Could these enzymes have radical mechanisms?

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Section: Acetolactate Synthase (Bacteria and Plants)mentioning

confidence: 96%

Oxygen toxicity from plants to people

Schloss

2002

Planta

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“…2 -mediated damage to Fe-S centres in enzymes involved in amino acid biosynthesis (Carlioz & Touati, 1986;Brown et al, 1995;Imlay, 2003) and the tricarboxylic acid pathway (Gardner & Fridovich, 1991;Liochev & Fridovich, 1993), and this growth defect can be overcome by the addition of exogenous amino acids to the growth medium (Carlioz & Touati, 1986). To determine if a similar deficiency in amino acid biosynthesis underlies the growth defect observed for the B. abortus sodA mutant, 2308, JB12 and JB12 [pSodA6] were cultured in a nutrient-limited medium with or without the addition of a mixture of all 20 amino acids.…”

Section: ?mentioning

confidence: 99%

SodA is a major metabolic antioxidant in Brucella abortus 2308 that plays a significant, but limited, role in the virulence of this strain in the mouse model

et al. 2012

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The gene designated BAB1_0591 in the Brucella abortus 2308 genome sequence encodes the manganese-cofactored superoxide dismutase SodA. An isogenic sodA mutant derived from B. abortus 2308, designated JB12, displays a small colony phenotype, increased sensitivity in vitro to endogenous superoxide generators, hydrogen peroxide and exposure to acidic pH, and a lag in growth when cultured in rich and minimal media that can be rescued by the addition of all 20 amino acids to the growth medium. B. abortus JB12 exhibits significant attenuation in both cultured murine macrophages and experimentally infected mice, but this attenuation is limited to the early stages of infection. Addition of the NADPH oxidase inhibitor apocynin to infected macrophages does not alleviate the attenuation exhibited by JB12, suggesting that the basis for the attenuation of the B. abortus sodA mutant is not an increased sensitivity to exogenous superoxide generated through the oxidative burst of host phagocytes. It is possible, however, that the increased sensitivity of the B. abortus sodA mutant to acid makes it less resistant than the parental strain to killing by the low pH encountered during the early stages of the development of the brucella-containing vacuoles in macrophages. These experimental findings support the proposed role for SodA as a major cytoplasmic antioxidant in brucella. Although this enzyme provides a clear benefit to B. abortus 2308 during the early stages of infection in macrophages and mice, SodA appears to be dispensable once the brucellae have established an infection.

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“…The O { 2 anion is known to attack enzymes with exposed [4Fe-4S] clusters, which results in the release of iron and loss of activity (Gardner & Fridovich, 1991;Brown et al, 1995). Furthermore, O { 2 directly inhibits the synthesis of cysteine and aromatic amino acids in Escherichia coli (Carlioz & Touati, 1986;Benov et al, 1996;Benov & Fridovich, 1999).…”

Section: Introductionmentioning

confidence: 99%

Transcriptome and proteome analysis of Bacillus subtilis gene expression in response to superoxide and peroxide stress

et al. 2004

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The Gram-positive soil bacterium Bacillus subtilis responds to oxidative stress by the activation of different cellular defence mechanisms. These are composed of scavenging enzymes as well as protection and repair systems organized in highly sophisticated networks. In this study, the peroxide and the superoxide stress stimulons of B. subtilis were characterized by means of transcriptomics and proteomics. The results demonstrate that oxidative-stress-responsive genes can be classified into two groups. One group encompasses genes which show similar expression patterns in the presence of both reactive oxygen species. Examples are members of the PerR and the Fur regulon which were induced by peroxide and superoxide stress. Similarly, both kinds of stress stimulated the activation of the stringent response. The second group is composed of genes primarily responding to one stimulus, like the members of the SOS regulon which were particularly upregulated in the presence of peroxide, and many genes involved in sulfate assimilation and methionine biosynthesis which were only induced by superoxide. Several genes encoding proteins of unknown function could be assigned to one of these groups.

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Dihydroxy-acid Dehydratase, a (4Fe-4S) Cluster-Containing Enzyme in Escherichia coli: Effects of Intracellular Superoxide Dismutase on Its Inactivation by Oxidant Stress

Cited by 37 publications

References 0 publications

Oxygen toxicity from plants to people

Oxygen toxicity from plants to people

SodA is a major metabolic antioxidant in Brucella abortus 2308 that plays a significant, but limited, role in the virulence of this strain in the mouse model

Transcriptome and proteome analysis of Bacillus subtilis gene expression in response to superoxide and peroxide stress

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