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Improving thermostability of (R)-selective amine transaminase from Aspergillus terreus through introduction of disulfide bonds.

Biotechnology and applied biochemistry - 1 Mar 2018

Xie Dong-Fang, Fang Hui, Mei Jia-Qi, Gong Jin-Yan, Wang Hong-Peng, Shen Xiu-Ying, Huang Jun, Mei Le-He

Abstract excerpt

To improve the thermostability of (R)-selective amine transaminase from Aspergillus terreus (AT-ATA), we used computer software Disulfide by Design and Modelling of Disulfide Bonds in Proteins to identify mutation sites where the disulfide bonds were most likely to form. We obtained three stabilized mutants (N25C-A28C, R131C-D134C, M150C-M280C) from seven candidates by site-directed mutagenesis. Compared to the...

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Aspergillus
Disulfides
Enzyme Stability
Mutagenesis, Site-Directed
Pyruvates

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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PMID: 28639260
DOI: 10.1002/bab.1572

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