Backbone and side chain 1H, 15N and 13C assignments for a thiol-disulphide oxidoreductase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125.
Enzymes produced by psychrophilic organisms have successfully overcome the low temperature challenge and evolved to maintain high catalytic rates in their permanently cold environments. As an initial step in our attempt to elucidate the cold-adaptation strategies used by these enzymes we report here the (1)H, (15)N and (13)C assignments for the reduced form of a thiol-disulphide oxidoreductase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125.
Collins
Tony
T
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, Apartado 127, 2780-156, Oeiras, Portugal.
Matzapetakis
Manolis
M
Santos
Helena
H
D000864:Antarctic Regions; D002247:Carbon Isotopes; D006859:Hydrogen; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D011490:Protein Disulfide Reductase (Glutathione) / Q000737:chemistry*; D017433:Protein Structure, Secondary; D031161:Pseudoalteromonas / Q000201:enzymology*; D013696:Temperature
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D006859:Hydrogen; D011490:Protein Disulfide Reductase (Glutathione)