Počet záznamů: 1  

Galactose Oxidase from Fusarium oxysporum - Expression in E. coli and P. pastoris and Biochemical Characterization

  1. 1.
    SYSNO ASEP0440666
    Druh ASEPJ - Článek v odborném periodiku
    Zařazení RIVJ - Článek v odborném periodiku
    Poddruh JČlánek ve WOS
    NázevGalactose Oxidase from Fusarium oxysporum - Expression in E. coli and P. pastoris and Biochemical Characterization
    Tvůrce(i) Paukner, R. (AT)
    Staudigl, P. (AT)
    Choosri, W. (TH)
    Sygmund, Ch. (AT)
    Halada, Petr (MBU-M) RID, ORCID
    Haltrich, D. (AT)
    Leitner, CH. (AT)
    Celkový počet autorů7
    Zdroj.dok.PLoS ONE. - : Public Library of Science - ISSN 1932-6203
    Roč. 9, č. 6 (2014)
    Poč.str.8 s.
    Jazyk dok.eng - angličtina
    Země vyd.US - Spojené státy americké
    Klíč. slovagalactose oxidase ; gene ; Fusarium ; gene expression
    Vědní obor RIVCE - Biochemie
    Institucionální podporaMBU-M - RVO:61388971
    UT WOS000338280800025
    AnotaceA gene coding for galactose 6-oxidase from Fusarium oxysporum G12 was cloned together with its native preprosequence and a C-terminal His-tag, and successfully expressed both in Escherichia coli and Pichia pastoris. The enzyme was subsequently purified and characterized. Among all tested substrates, the highest catalytic efficiency (k(cat)/K-m) was found with 1-methyl-beta-D-galactopyranoside (2.2 mM(-1) s(-1)). The Michaelis constant (K-m) for D-galactose was determined to be 47 mM. Optimal pH and temperature for the enzyme activity were 7.0 and 40 degrees C, respectively, and the enzyme was thermoinactivated at temperatures above 50 degrees C. GalOx contains a unique metalloradical complex consisting of a copper atom and a tyrosine residue covalently attached to the sulphur of a cysteine. The correct formation of this thioether bond during the heterologous expression in E. coli and P. pastoris could be unequivocally confirmed by MALDI mass spectrometry, which offers a convenient alternative to prove this Tyr-Cys crosslink, which is essential for the catalytic activity of GalOx.
    PracovištěMikrobiologický ústav
    KontaktEliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231
    Rok sběru2015
Počet záznamů: 1  

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