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Backbone and side chain 1H, 15N and 13C assignments for a thiol-disulphide oxidoreductase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125

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Abstract

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 1H, 15N and 13C assignments for the reduced form of a thiol-disulphide oxidoreductase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125.

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Acknowledgments

The NMR spectrometers are part of The National NMR Network (REDE/1517/RMN/2005), supported by “Programa Operacional Ciência e Inovação (POCTI) 2010” and Fundação para a Ciência e a Tecnologia (FCT). This work was funded by FCT, POCTI and FEDER; Projects POCI/BIA-PRO/57263/2004 and PTDC/BIO/70806/2006. TC is holder of a long term EMBO fellowship. MM is thankful to the Fundação para a Ciência e Tecnologia for its support through Programa Ciência 2007.

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  1. Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, Apartado 127, 2780-156, Oeiras, Portugal

    Tony Collins, Manolis Matzapetakis & Helena Santos

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  1. Tony Collins
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  2. Manolis Matzapetakis
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  3. Helena Santos
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Correspondence to Manolis Matzapetakis.

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Collins, T., Matzapetakis, M. & Santos, H. Backbone and side chain 1H, 15N and 13C assignments for a thiol-disulphide oxidoreductase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125. Biomol NMR Assign 4, 151–154 (2010). https://doi.org/10.1007/s12104-010-9230-0

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  • DOI: https://doi.org/10.1007/s12104-010-9230-0

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