Analysis of self-catalytic maturation capability of galactose oxidase by site-directed mutagenesis

Date

2010-06-01

Author

Kocuklu, B.
Ögel, Zümrüt Begüm
McPherson, M. J.

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https://hdl.handle.net/11511/53813

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Graduate School of Natural and Applied Sciences, Conference / Seminar

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Analysis of self-processing mechanism of galactose oxidase by site-directed mutagenesis and heterologous expression in Escherichia Coli Gençer, Burçak; Ögel, Zümrüt Begüm; Department of Biotechnology (2005) In this study, self-catalytic maturation of heterologously expressed pro-galactose oxidase was analysed in E.coli by altering some amino acids which were supposed to play a crucial role in pro-peptide removal. Galactose oxidase (GOase; EC 1.1.3.9) from Fusarium graminearum; having a molecular mass of 68kDa, is a monomeric, copper containing enzyme with an unusual thioether bond. The enzyme is produced as a precursor with an additional 8 amino acid pre- and a 17- amino acid pro-sequence at the N terminus. Pr...
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Citation Formats

B. Kocuklu, Z. B. Ögel, and M. J. McPherson, “Analysis of self-catalytic maturation capability of galactose oxidase by site-directed mutagenesis,” 2010, vol. 277, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/53813.