Article
The structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability.
Acta crystallographica. Section D, Biological crystallography - 1 Jun 2003
Houborg Karen, Harris Pernille, Poulsen Jens-Christian Navarro, Schneider Palle, Svendsen Allan, Larsen Sine
Abstract excerpt
Seven amino-acid substitutions introduced into the 343 amino-acid-long sequence of Coprinus cinereus peroxidase (CiP) led to a mutant enzyme (TS-rCiP) which is more stable than the native enzyme at higher temperature, pH and hydrogen peroxide concentrations. It is therefore more suitable for industrial applications. A structure determination was conducted on a deglycosylated but still active form of TS-rCiP based...
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