Asp477 is a determinant of the enantioselectivity in yeast transketolase

FEBS Letters
U NilssonG Schneider

Abstract

The conserved residue Asp477 in yeast transketolase is located in the substrate channel of the enzyme and forms a hydrogen bond with the C2-hydroxyl group of the acceptor substrate. The significance of this interaction for the recognition of the preferred acceptor substrates, D-alpha-hydroxyaldehydes was investigated by site-directed mutagenesis. In the wild-type enzyme the kcat/KM values are by three to four orders of magnitude lower for 2-deoxyaldoses or substrates with L-configuration at the C2-atom. In the Asp477 Ala mutant, the kcat/KM values for D-alpha-hydroxyaldehydes are decreased by a thousandfold, while the kcat/KM values for substrates with L-configuration or 2-deoxyaldoses are similar to wild-type enzyme. These results indicate that Asp477 is involved in determining the enantioselectivity of transketolase.

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Citations

Nov 29, 2007·Journal of Molecular Evolution·Seán J CostelloePaul A Dalby
Dec 5, 2000·Current Opinion in Biotechnology·N J Turner
Nov 11, 2010·BMC Plant Biology·Francesco EmanuelliMaria S Grando
Apr 19, 2003·Physiologia Plantarum·Dring N. CrowellS. Narasimha Chary
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Nov 22, 2014·Chemical Communications : Chem Comm·Dong YiWolf-Dieter Fessner
Sep 17, 2013·The FEBS Journal·Helen C HailesMartina Pohl
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Oct 20, 2012·Organic & Biomolecular Chemistry·Panwajee PayongsriPaul A Dalby
Jul 24, 2012·Chembiochem : a European Journal of Chemical Biology·Adeline RanouxUlf Hanefeld
Jun 11, 2002·Biochemical and Biophysical Research Communications·Marina V KovinaGerman A Kochetov
Mar 23, 2011·Chemical Reviews·Margarita BrovettoGustavo A Seoane

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