Rational substrate and enzyme engineering of transketolase for aromatics.
The uses of 3-formylbenzoic acid and 4-formylbenzoic acid as molecular probes along with previous and new transketolase mutants revealed the factors governing the rate of reaction between transketolase and aromatic aldehydes. The novel α,α-dihydroxyketones were produced at 15 to 30-fold higher yields and up to 250-fold higher specific activities with D469T TK when compared to those obtained for benzaldehyde.
Advanced Centre for Biochemical Engineering, Department of Biochemical Engineering, University College London, Torrington Place, London, WC1E 7JE, UK.
Panwajee
P
Payongsri
David
D
Steadman
John
J
Strafford
Andrew
A
MacMurray
Helen C
HC
Hailes
Paul A
PA
Dalby
D019817:Benzoic Acid / Q000737:chemistry* / Q000378:metabolism*; D020134:Catalytic Domain; D004926:Escherichia coli / Q000201:enzymology; D006860:Hydrogen Bonding; D007700:Kinetics; D062105:Molecular Docking Simulation; D009154:Mutation; D015202:Protein Engineering / Q000379:methods*; D055672:Static Electricity; D014174:Transketolase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*
D019817:Benzoic Acid; D014174:Transketolase