Effects of the polyhistidine tag on kinetics and other properties of trehalose synthase from Deinococcus geothermalis. | Zendy

Anna Panek | Zendy; Olga Pietrow | Zendy; Paweł Filipkowski | Zendy; Józef Synowiecki | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Effects of the polyhistidine tag on kinetics and other properties of trehalose synthase from Deinococcus geothermalis.

Author(s) -

Anna Panek,

Olga Pietrow,

Paweł Filipkowski,

Józef Synowiecki

Publication year - 2013

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.2013_1966

Subject(s) - trehalose , atp synthase , chemistry , histidine , recombinant dna , biochemistry , maltose , sulfolobus acidocaldarius , enzyme , archaea , gene

Two recombinant trehalose synthases from Deinococcus geothermalis (DSMZ 11300) were compared. A significant influence of the artificial polyhistidine tag was observed in protein constitution. The recombinant trehalose synthase from D. geothermalis with His₆-tag has a higher Km value of 254 mM, in comparison with the wild-type trehalose synthase (Km 170 mM), and displayed a lower activity of maltose conversion when compared to the wild type. Moreover, differences in properties like temperature, pH, thermal- and pH-stability were observed. Presence of the histidine tag caused a decrease of thermal resistance in case of trehalose synthase with His₆-tag. These data confirmed a suggestion that the introduction of the histidine domain produces in some seldom cases undesirable changes in the protein.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research