scholarly journals Aspartate aminotransferase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC 125

2000 ◽  
Vol 267 (9) ◽  
pp. 2790-2802 ◽  
Author(s):  
Leila Birolo ◽  
M. Luisa Tutino ◽  
Bianca Fontanella ◽  
Charles Gerday ◽  
Katia Mainolfi ◽  
...  
Keyword(s):  
Aspartate Aminotransferase ◽  
Pseudoalteromonas Haloplanktis ◽  
Antarctic Bacterium ◽  
The Antarctic

Cold-adapted bacteria and the globin case study in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125

2010 ◽  
Vol 3 (3-4) ◽  
pp. 125-131 ◽  
Author(s):  
Roberta Russo ◽  
Daniela Giordano ◽  
Alessia Riccio ◽  
Guido di Prisco ◽  
Cinzia Verde
Keyword(s):  
Cold Adapted ◽  
Pseudoalteromonas Haloplanktis ◽  
Antarctic Bacterium ◽  
Pseudoalteromonas Haloplanktis Tac125 ◽  
The Antarctic

Cloning, characterization and anion inhibition studies of a new γ-carbonic anhydrase from the Antarctic bacterium Pseudoalteromonas haloplanktis

2015 ◽  
Vol 23 (15) ◽  
pp. 4405-4409 ◽  
Author(s):  
Viviana De Luca ◽  
Daniela Vullo ◽  
Sonia Del Prete ◽  
Vincenzo Carginale ◽  
Andrea Scozzafava ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Pseudoalteromonas Haloplanktis ◽  
Antarctic Bacterium ◽  
Inhibition Studies ◽  
The Antarctic

Ligand-rebinding kinetics of 2/2 hemoglobin from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125

2013 ◽  
Vol 1834 (9) ◽  
pp. 1932-1938 ◽  
Author(s):  
Roberta Russo ◽  
Daniela Giordano ◽  
Guido di Prisco ◽  
Gaston Hui Bon Hoa ◽  
Michael C. Marden ◽  
...  
Keyword(s):  
Pseudoalteromonas Haloplanktis ◽  
Antarctic Bacterium ◽  
Pseudoalteromonas Haloplanktis Tac125 ◽  
Ligand Rebinding ◽  
The Antarctic ◽  
Kinetics Of

scholarly journals Sulfonamide inhibition studies of the γ-carbonic anhydrase from the Antarctic bacterium Pseudoalteromonas haloplanktis

2015 ◽  
Vol 25 (17) ◽  
pp. 3550-3555 ◽  
Author(s):  
Daniela Vullo ◽  
Viviana De Luca ◽  
Sonia Del Prete ◽  
Vincenzo Carginale ◽  
Andrea Scozzafava ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Pseudoalteromonas Haloplanktis ◽  
Antarctic Bacterium ◽  
Inhibition Studies ◽  
The Antarctic

scholarly journals Influence of Growth Temperature on Lipid and Phosphate Contents of Surface Polysaccharides from the Antarctic Bacterium Pseudoalteromonas haloplanktis TAC 125

2004 ◽  
Vol 186 (1) ◽  
pp. 29-34 ◽  
Author(s):  
M. Michela Corsaro ◽  
Rosa Lanzetta ◽  
Ermenegilda Parrilli ◽  
Michelangelo Parrilli ◽  
M. Luisa Tutino ◽  
...  
Keyword(s):  
Growth Temperature ◽  
Lipid A ◽  
Optimal Growth ◽  
Structural Variations ◽  
Optimal Growth Temperature ◽  
Pseudoalteromonas Haloplanktis ◽  
Antarctic Bacterium ◽  
Surface Polysaccharides ◽  
The Antarctic ◽  
Two Temperature

ABSTRACT The chemical structural variations induced by different growth temperatures in the lipooligosaccharide and exopolysaccharide components extracted from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC 125 are described. The increase in phosphorylation with the increase in growth temperature seems to be general, because it happens not only for the lipooligosaccharide but also for the exopolysaccharide. Structural variations in the lipid components of lipid A also occur. In addition, free lipid A is found at both 25 and 4°C but not at 15°C, which is the optimal growth temperature, suggesting a incomplete biosynthesis of the lipooligosaccharide component under the first two temperature conditions.

The cold-active Lip1 lipase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 is a member of a new bacterial lipolytic enzyme family

Extremophiles ◽  
2008 ◽  
Vol 12 (3) ◽  
pp. 311-323 ◽  
Author(s):  
Donatella de Pascale ◽  
Angela M. Cusano ◽  
Flavia Autore ◽  
Ermenegilda Parrilli ◽  
Guido di Prisco ◽  
...  
Keyword(s):  
Lipolytic Enzyme ◽  
Pseudoalteromonas Haloplanktis ◽  
Antarctic Bacterium ◽  
Pseudoalteromonas Haloplanktis Tac125 ◽  
Enzyme Family ◽  
Cold Active ◽  
The Antarctic

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

2004 ◽  
Vol 384 (2) ◽  
pp. 247-253 ◽  
Author(s):  
Geneviève GARSOUX ◽  
Josette LAMOTTE ◽  
Charles GERDAY ◽  
Georges FELLER
Keyword(s):  
Active Site ◽  
Low Temperatures ◽  
Catalytic Domain ◽  
Homology Modelling ◽  
Temperature Adaptation ◽  
Substrate Affinity ◽  
Structural Factors ◽  
Pseudoalteromonas Haloplanktis ◽  
Antarctic Bacterium ◽  
The Antarctic

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 and expressed in Escherichia coli. This cellulase is composed of three structurally and functionally distinct regions: an N-terminal catalytic domain belonging to glycosidase family 5 and a C-terminal cellulose-binding domain belonging to carbohydrate-binding module family 5. The linker of 107 residues connecting both domains is one of the longest found in cellulases, and optimizes substrate accessibility to the catalytic domain by drastically increasing the surface of cellulose available to a bound enzyme molecule. The psychrophilic enzyme is closely related to the cellulase Cel5 from Erwinia chrysanthemi. Both kcat and kcat/Km values at 4 °C for the psychrophilic cellulase are similar to the values for Cel5 at 30–35 °C, suggesting temperature adaptation of the kinetic parameters. The thermodynamic parameters of activation of CelG suggest a heat-labile, relatively disordered active site with low substrate affinity, in agreement with the experimental data. The structure of CelG has been constructed by homology modelling with a molecule of cellotetraose docked into the active site. No structural alteration related to cold-activity can be found in the catalytic cleft, whereas several structural factors in the overall structure can explain the weak thermal stability, suggesting that the loss of stability provides the required active-site mobility at low temperatures.

scholarly journals Coexistence of multiple globin genes conferring protection against nitrosative stress to the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125

Nitric Oxide ◽  
2018 ◽  
Vol 73 ◽  
pp. 39-51 ◽  
Author(s):  
Daniela Coppola ◽  
Daniela Giordano ◽  
Lisa Milazzo ◽  
Barry D. Howes ◽  
Paolo Ascenzi ◽  
...  
Keyword(s):  
Nitrosative Stress ◽  
Globin Genes ◽  
Pseudoalteromonas Haloplanktis ◽  
Antarctic Bacterium ◽  
Pseudoalteromonas Haloplanktis Tac125 ◽  
The Antarctic
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