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See detailKinetic and structural optimization to catalysis at low temperatures in a psychrophilic cellulase from the Antarctic bacterium Pseudoalteromonas haloplanktis
Garsoux, G.; Lamotte, J.; Gerday, Charles ULg et al

in Biochemical Journal (2004), 384(Pt 2), 247-253

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 ... [more ▼]

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 k(cat) and k(cat)/K-m values at 4 degreesC for the psychrophilic cellulase are similar to the values for Cel5 at 30-35 degreesC, 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. [less ▲]

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See detailCold enzymes : a hot topic
Gerday, Charles ULg; Aittaleb, M.; Arpigny, J. L. et al

in Margesin, R.; Schinner, F. (Eds.) Cold-adapted Organisms : Ecology, Physiology, Enzymology and Molecular Biology (1999)

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See detailPsychrophiles et thermophiles : un problème d’enzyme
Gerday, Charles ULg; Aittaleb, M.; Arpigny, J. L. et al

in Chimie Nouvelle (1997), 15

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See detailSpecific transcription factors control the c-erbB2 gene expression in the mammary tumor BT-474 cells.
Grooteclaes, Madeleine; Pasleau, Françoise ULg; Garsoux, G. et al

Conference (1995, December)

Detailed reference viewed: 17 (1 ULg)