The pH optimum of native uracil - DNA glycosylase of Archaeoglobus fulgidus compared to recombinant enzyme indicates adaption to cytosolic pH

• Autorzy: Knaevelsrud I. , Kazazic S. , Birkeland N. K. , Bjelland S.
• Języki publikacji: EN

Abstrakty

EN

 Uracil-DNA glycosylase of Archaeoglobus fulgidus (Afung) in cell extracts exhibited maximal activity around pH 6.2 as compared to pH 4.8 for the purified recombinant enzyme expressed in Escherichia coli. Native Afung thus seems to be adapted to the intracellular pH of A. fulgidus, determined to be 7.0±0.1. Both recombinant and native Afung exhibited a broad temperature optimum for activity around 80°C, reflecting the A. fulgidus optimal growth temperature of 83°C. Adaption to the neutral conditions in the A. fulgidus cytoplasm might be due to covalent modifications or accessory factors, or due to a different folding when expressed in the native host.

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2014
• Tom: 61
• Numer: 2
• Opis fizyczny: p.393-395,fig.,ref.

Twórcy

autor

Knaevelsrud I.

• Faculty of Science and Technology, Department of Mathematics and Natural Sciences-Centre for Organelle Research, University of Stavanger, Stavanger, Norway
• Department of Biology and Centre for Geobiology, University of Bergen, Bergen, Norway

autor

Kazazic S.

• Faculty of Science and Technology, Department of Mathematics and Natural Sciences-Centre for Organelle Research, University of Stavanger, Stavanger, Norway

autor

Birkeland N. K.

• Department of Biology and Centre for Geobiology, University of Bergen, Bergen, Norway

autor

Bjelland S.

• Faculty of Science and Technology, Department of Mathematics and Natural Sciences-Centre for Organelle Research, University of Stavanger, Stavanger, Norway

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