Charles Gerday

Enzyme activity determination on macromolecular substrates by isothermal titration calorimetry: application to mesophilic and psychrophilic chitinases (2001)

Lonhienne, Thierry, Baise, Etienne, Feller, Georges, Bouriotis, Vassilis, Gerday, Charles

Isothermal titration calorimetry has been applied to the determination of the kinetic parameters of chitinases (EC 3.2.1.14) by monitoring the heat released during the hydrolysis of chitin glycosidic...

Modular structure, local flexibility and cold-activity of a novel chitobiase from a psychrophilic Antarctic bacterium (2001)

Lonhienne, Thierry, Zoidakis, Jérôme, Vorgias, Constantinos E., Feller, Georges, Gerday, Charles, Bouriotis, Vassilis

The gene archb encoding for the cell-bound chitobiase from the Antarctic Gram-positive bacterium Arthrobacter sp. TAD20 was cloned and expressed in Escherichia coli in a soluble form. The mature...

Cloning, sequences, and characterization of two chitinase genes from the antarctic Arthrobacter sp strain TAD20: Isolation and partial characterization of the enzymes (2001)

Lonhienne, Thierry, Mavromatis, Konstantinos, Vorgias, Constantin E., Buchon, Laurent, Gerday, Charles, Bouriotis, Vassilis

Arthrobacter sp. strain TAD20, a chitinolytic gram-positive organism, was isolated from the sea bottom along the Antarctic ice shell. Arthrobacter sp. strain TAD20 secretes two major chitinases, ChiA...

Cloning, Sequences, and Characterization of Two Chitinase Genes from the Antarctic Arthrobacter sp. Strain TAD20: Isolation and Partial Characterization of the Enzymes

Lonhienne, Thierry, Mavromatis, Konstantinos, Vorgias, Constantin E., Buchon, Laurent, Gerday, Charles, Bouriotis, Vassilis

Arthrobacter sp. strain TAD20, a chitinolytic gram-positive organism, was isolated from the sea bottom along the Antarctic ice shell. Arthrobacter sp. strain TAD20 secretes two major chitinases, ChiA...

Expression of Psychrophilic Genes in Mesophilic Hosts: Assessment of the Folding State of a Recombinant α-Amylase

Feller, Georges, Le Bussy, Olivier, Gerday, Charles

α-Amylase from the antarctic psychrophile Alteromonas haloplanktis is synthesized at 0 ± 2°C by the wild strain. This heat-labile α-amylase folds correctly when overexpressed in Escherichia coli,...

Metabolic Enzymes from Psychrophilic Bacteria: Challenge of Adaptation to Low Temperatures in Ornithine Carbamoyltransferase from Moritella abyssi

Xu, Ying, Feller, Georges, Gerday, Charles, Glansdorff, Nicolas

The enzyme ornithine carbamoyltransferase (OTCase) of Moritella abyssi (OTCaseMab), a new, strictly psychrophilic and piezophilic bacterial species, was purified. OTCaseMab displays maximal activity...

Moritella Cold-Active Dihydrofolate Reductase: Are There Natural Limits to Optimization of Catalytic Efficiency at Low Temperature?

Xu, Ying, Feller, Georges, Gerday, Charles, Glansdorff, Nicolas

Adapting metabolic enzymes of microorganisms to low temperature environments may require a difficult compromise between velocity and affinity. We have investigated catalytic efficiency in a key...

Kinetic and structural optimization to catalysis at low temperatures in a psychrophilic cellulase from the Antarctic bacterium Pseudoalteromonas haloplanktis

Garsoux, Geneviève, Lamotte, Josette, Gerday, Charles, Feller, Georges

The cold-adapted cellulase CelG has been purified from the culture supernatant of the Antarctic bacterium Pseudoalteromonas haloplanktis and the gene coding for this enzyme has been cloned, sequenced...

The Active Site Is the Least Stable Structure in the Unfolding Pathway of a Multidomain Cold-Adapted α-Amylase

Siddiqui, Khawar S., Feller, Georges, D'Amico, Salvino, Gerday, Charles, Giaquinto, Laura, Cavicchioli, Ricardo

The cold-active α-amylase from the Antarctic bacterium Pseudoalteromonas haloplanktis (AHA) is the largest known multidomain enzyme that displays reversible thermal unfolding (around 30°C)...

Role of Disulfide Bridges in the Activity and Stability of a Cold-Active α-Amylase

Siddiqui, Khawar Sohail, Poljak, Anne, Guilhaus, Michael, Feller, Georges, D'Amico, Salvino, Gerday, Charles, ...

The cold-adapted α-amylase from Pseudoalteromonas haloplanktis unfolds reversibly and cooperatively according to a two-state mechanism at 30°C and unfolds reversibly and sequentially with two...

Adenylation-Dependent Conformation and Unfolding Pathways of the NAD+-Dependent DNA Ligase from the Thermophile Thermus scotoductus

Georlette, Daphné, Blaise, Vinciane, Bouillenne, Fabrice, Damien, Benjamin, Thorbjarnardóttir, Sigridur H., Depiereux, Eric, ...

In the last few years, an increased attention has been focused on NAD+-dependent DNA ligases. This is mostly due to their potential use as antibiotic targets, because effective inhibition of these...

Cloning, Sequences, and Characterization of Two Chitinase Genes from the Antarctic Arthrobacter sp. Strain TAD20: Isolation and Partial Characterization of the Enzymes

Lonhienne, Thierry, Mavromatis, Konstantinos, Vorgias, Constantin E., Buchon, Laurent, Gerday, Charles, Bouriotis, Vassilis

Arthrobacter sp. strain TAD20, a chitinolytic gram-positive organism, was isolated from the sea bottom along the Antarctic ice shell. Arthrobacter sp. strain TAD20 secretes two major chitinases, ChiA...

Expression of Psychrophilic Genes in Mesophilic Hosts: Assessment of the Folding State of a Recombinant α-Amylase

Feller, Georges, Le Bussy, Olivier, Gerday, Charles

α-Amylase from the antarctic psychrophile Alteromonas haloplanktis is synthesized at 0 ± 2°C by the wild strain. This heat-labile α-amylase folds correctly when overexpressed in Escherichia coli,...

Metabolic Enzymes from Psychrophilic Bacteria: Challenge of Adaptation to Low Temperatures in Ornithine Carbamoyltransferase from Moritella abyssi

Xu, Ying, Feller, Georges, Gerday, Charles, Glansdorff, Nicolas

The enzyme ornithine carbamoyltransferase (OTCase) of Moritella abyssi (OTCaseMab), a new, strictly psychrophilic and piezophilic bacterial species, was purified. OTCaseMab displays maximal activity...

Moritella Cold-Active Dihydrofolate Reductase: Are There Natural Limits to Optimization of Catalytic Efficiency at Low Temperature?

Xu, Ying, Feller, Georges, Gerday, Charles, Glansdorff, Nicolas

Adapting metabolic enzymes of microorganisms to low temperature environments may require a difficult compromise between velocity and affinity. We have investigated catalytic efficiency in a key...

Kinetic and structural optimization to catalysis at low temperatures in a psychrophilic cellulase from the Antarctic bacterium Pseudoalteromonas haloplanktis

Garsoux, Geneviève, Lamotte, Josette, Gerday, Charles, Feller, Georges

The cold-adapted cellulase CelG has been purified from the culture supernatant of the Antarctic bacterium Pseudoalteromonas haloplanktis and the gene coding for this enzyme has been cloned, sequenced...

The Active Site Is the Least Stable Structure in the Unfolding Pathway of a Multidomain Cold-Adapted α-Amylase

Siddiqui, Khawar S., Feller, Georges, D'Amico, Salvino, Gerday, Charles, Giaquinto, Laura, Cavicchioli, Ricardo

The cold-active α-amylase from the Antarctic bacterium Pseudoalteromonas haloplanktis (AHA) is the largest known multidomain enzyme that displays reversible thermal unfolding (around 30°C)...

Role of Disulfide Bridges in the Activity and Stability of a Cold-Active α-Amylase

Siddiqui, Khawar Sohail, Poljak, Anne, Guilhaus, Michael, Feller, Georges, D'Amico, Salvino, Gerday, Charles, ...

The cold-adapted α-amylase from Pseudoalteromonas haloplanktis unfolds reversibly and cooperatively according to a two-state mechanism at 30°C and unfolds reversibly and sequentially with two...

Adenylation-Dependent Conformation and Unfolding Pathways of the NAD+-Dependent DNA Ligase from the Thermophile Thermus scotoductus

Georlette, Daphné, Blaise, Vinciane, Bouillenne, Fabrice, Damien, Benjamin, Thorbjarnardóttir, Sigridur H., Depiereux, Eric, ...

In the last few years, an increased attention has been focused on NAD+-dependent DNA ligases. This is mostly due to their potential use as antibiotic targets, because effective inhibition of these...

Molecular basis of cold adaptation.

D'Amico, Salvino, Claverie, Paule, Collins, Tony, Georlette, Daphné, Gratia, Emmanuelle, Hoyoux, Anne, ...

Cold-adapted, or psychrophilic, organisms are able to thrive at low temperatures in permanently cold environments, which in fact characterize the greatest proportion of our planet. Psychrophiles...

Psychrophilic microorganisms: challenges for life

D'Amico, Salvino, Collins, Tony, Marx, Jean-Claude, Feller, Georges, Gerday, Charles

The ability of psychrophiles to survive and proliferate at low temperatures implies that they have overcome key barriers inherent to permanently cold environments. These challenges include: reduced...

The linker region plays a key role in the adaptation to cold of the cellulase from an Antarctic bacterium

Sonan, Guillaume K., Receveur-Brechot, Véronique, Duez, Colette, Aghajari, Nushin, Czjzek, Mirjam, Haser, Richard, ...

The psychrophilic cellulase, Cel5G, from the Antarctic bacterium Pseudoalteromonas haloplanktis is composed of a catalytic module (CM) joined to a carbohydrate-binding module (CBM) by an unusually...

Structural basis of α-amylase activation by chloride

Aghajari, Nushin, Feller, Georges, Gerday, Charles, Haser, Richard

To further investigate the mechanism and function of allosteric activation by chloride in some α-amylases, the structure of the bacterial α-amylase from the psychrophilic micro-organism...