Properties of the endogenous components of the thioredoxin system in the psychrophilic eubacterium Pseudoalteromonas haloplanktis TAC 125

Falasca, Patrizia; Evangelista, Giovanna; Cotugno, Roberta; Marco, Salvatore; Vendittis, Emmanuele De; Raimo, Gennaro

doi:10.1007/s00792-012-0453-0

Cited by 14 publications

(15 citation statements)

References 50 publications

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“…It has been suggested that this chaperonin remains suited to function during sudden temperature increases of the environment [83]. Similarly, activity of thioredoxin from the same bacterium is much more heat stable than that of E. coli [292, 293]. One cannot exclude that enzymes involved in electron transfer do not require the same type of adaptations because the rate of electron flow is not significantly affected by the low biological temperatures.…”

Section: Activity-flexibility-stability Relationships: Current Issuesmentioning

confidence: 99%

Psychrophilic Enzymes: From Folding to Function and Biotechnology

2013

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Psychrophiles thriving permanently at near-zero temperatures synthesize cold-active enzymes to sustain their cell cycle. Genome sequences, proteomic, and transcriptomic studies suggest various adaptive features to maintain adequate translation and proper protein folding under cold conditions. Most psychrophilic enzymes optimize a high activity at low temperature at the expense of substrate affinity, therefore reducing the free energy barrier of the transition state. Furthermore, a weak temperature dependence of activity ensures moderate reduction of the catalytic activity in the cold. In these naturally evolved enzymes, the optimization to low temperature activity is reached via destabilization of the structures bearing the active site or by destabilization of the whole molecule. This involves a reduction in the number and strength of all types of weak interactions or the disappearance of stability factors, resulting in improved dynamics of active site residues in the cold. These enzymes are already used in many biotechnological applications requiring high activity at mild temperatures or fast heat-inactivation rate. Several open questions in the field are also highlighted.

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Section: Activity-flexibility-stability Relationships: Current Issuesmentioning

confidence: 99%

Psychrophilic Enzymes: From Folding to Function and Biotechnology

2013

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“…It has been suggested that this chaperonin remains suited to function during sudden temperature increases of the environment [21]. Similarly, activity of thioredoxin from the same bacterium is much more heat-stable than that of E. coli [22]. One cannot exclude the possibility that enzymes involved in electron transfer do not require the same type of adaptations because the rate of electron flow is not significantly affected by the low biological temperatures.…”

Section: Kinetic Properties Of Cold Enzymesmentioning

confidence: 99%

Optimization to Low Temperature Activity in Psychrophilic Enzymes

Struvay

Feller

2012

IJMS

212

152

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Psychrophiles, i.e., organisms thriving permanently at near-zero temperatures, synthesize cold-active enzymes to sustain their cell cycle. These enzymes are already used in many biotechnological applications requiring high activity at mild temperatures or fast heat-inactivation rate. Most psychrophilic enzymes optimize a high activity at low temperature at the expense of substrate affinity, therefore reducing the free energy barrier of the transition state. Furthermore, a weak temperature dependence of activity ensures moderate reduction of the catalytic activity in the cold. In these naturally evolved enzymes, the optimization to low temperature activity is reached via destabilization of the structures bearing the active site or by destabilization of the whole molecule. This involves a reduction in the number and strength of all types of weak interactions or the disappearance of stability factors, resulting in improved dynamics of active site residues in the cold. Considering the subtle structural adjustments required for low temperature activity, directed evolution appears to be the most suitable methodology to engineer cold activity in biological catalysts.

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“…CF6-2 in particular being studied in more detail [31,33]. The cold adaptation properties of Pseudoalteromonas haloplanktis TAC125 have been described with respect to its thioredoxin system [37,38] and the involvement of a single highly-active iron superoxide dismutase as a reactive oxygen species defense mechanism [39,40]. With this in mind, this study focused on the isolation and comparative genomics of three non-pigmented Pseudoalteromonas spp.…”

Section: Introductionmentioning

confidence: 99%

Biotechnological Potential of Cold Adapted Pseudoalteromonas spp. Isolated from ‘Deep Sea’ Sponges

et al. 2017

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The marine genus Pseudoalteromonas is known for its versatile biotechnological potential with respect to the production of antimicrobials and enzymes of industrial interest. We have sequenced the genomes of three Pseudoalteromonas sp. strains isolated from different deep sea sponges on the Illumina MiSeq platform. The isolates have been screened for various industrially important enzymes and comparative genomics has been applied to investigate potential relationships between the isolates and their host organisms, while comparing them to free-living Pseudoalteromonas spp. from shallow and deep sea environments. The genomes of the sponge associated Pseudoalteromonas strains contained much lower levels of potential eukaryotic-like proteins which are known to be enriched in symbiotic sponge associated microorganisms, than might be expected for true sponge symbionts. While all the Pseudoalteromonas shared a large distinct subset of genes, nonetheless the number of unique and accessory genes is quite large and defines the pan-genome as open. Enzymatic screens indicate that a vast array of enzyme activities is expressed by the isolates, including β-galactosidase, β-glucosidase, and protease activities. A β-glucosidase gene from one of the Pseudoalteromonas isolates, strain EB27 was heterologously expressed in Escherichia coli and, following biochemical characterization, the recombinant enzyme was found to be cold-adapted, thermolabile, halotolerant, and alkaline active.

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Properties of the endogenous components of the thioredoxin system in the psychrophilic eubacterium Pseudoalteromonas haloplanktis TAC 125

Cited by 14 publications

References 50 publications

Psychrophilic Enzymes: From Folding to Function and Biotechnology

Psychrophilic Enzymes: From Folding to Function and Biotechnology

Optimization to Low Temperature Activity in Psychrophilic Enzymes

Biotechnological Potential of Cold Adapted Pseudoalteromonas spp. Isolated from ‘Deep Sea’ Sponges

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