Transketolase mutants previously identified for use with the non-phosphorylated aldehyde propanal have been explored with a series of linear and cyclic aliphatic aldehydes, and excellent stereoselectivities observed.
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http://dx.doi.org/10.1039/b924144b | DOI Listing |
Chembiochem
March 2017
State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Meilong Road 130, 200237, Shanghai, P.R. China.
The transketolase from Geobacillus stearothermophilus (TK ) is a thermostable enzyme with notable high activity and stability at elevated temperatures, but it accepts non-α-hydroxylated aldehydes only with low efficiency. Here we report a protein engineering study of TK based on double-site saturation mutagenesis either at Leu191 or at Phe435 in combination with Asp470; these are the residues responsible for substrate binding in the active site. Screening of the mutagenesis libraries resulted in several positive variants with activity towards propanal up to 7.
View Article and Find Full Text PDFOrg Biomol Chem
March 2010
Department of Chemistry, University College London, 20 Gordon Street, London, UK WC1H 0AJ.
Transketolase mutants previously identified for use with the non-phosphorylated aldehyde propanal have been explored with a series of linear and cyclic aliphatic aldehydes, and excellent stereoselectivities observed.
View Article and Find Full Text PDFBioorg Med Chem
October 2006
Department of Chemistry, University College London, 20 Gordon Street, London WC1H OAJ, UK.
A tetrazolium red-based colorimetric assay has been devised to screen for transketolase activity with a range of aldehyde acceptors. The colorimetric TK assay is able to detect >8% bioconversion using non-alpha-hydroxylated aldehydes as acceptor substrates and is significantly faster and more convenient to use than chromatographic procedures.
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